scholarly journals Structural organization and evolution of the marsupial zona pellucida

Reproduction ◽  
2002 ◽  
pp. 13-21 ◽  
Author(s):  
WG Breed ◽  
RM Hope ◽  
OW Wiebkin ◽  
SC Spargo ◽  
JA Chapman
Keyword(s):  
Zona Pellucida ◽  
Structural Organization ◽  
Sequence Similarity ◽  
Phylogenetic Analyses ◽  
Three Dimensional ◽  
Reducing Agents ◽  
Molecular Organization ◽  
Dimensional Structure ◽  
High Sequence Similarity ◽  
Lectin Staining

In this review, the biochemical composition and structural organization of the marsupial and eutherian zonae pellucidae are compared. Differences between the zonae from these two groups of mammals are observed in their response to dilute proteases and reducing agents, in their potential glycosylation patterns, and in some of their functions. However, studies on the glycoconjugates and polypeptides of the three zona pellucida genes have not explained these different responses to the proteases and reducing agents. There is high sequence similarity between the zona polypeptides of marsupials and eutherians, as well as a similarity in the oligosaccharides present, as demonstrated by lectin staining. As the marsupial and eutherian lineages diverged from a common ancestor over 100 million years ago, these observations indicate that the three-dimensional structure of these glycoproteins is highly conserved throughout all mammals, although the complexity of its molecular organization has yet to be resolved. Phylogenetic analyses indicate that there are at least four groups of paralogous zona pellucida genes in vertebrates. The marsupial ZPA and ZPB genes have been named in accordance with their orthologues but the phylogenetic relationships of the marsupial ZPC gene require further investigation.

scholarly journals Defensin-like peptide-2 from platypus venom: member of a class of peptides with a distinct structural fold

2000 ◽  
Vol 348 (3) ◽  
pp. 649-656 ◽  
Author(s):  
Allan M. TORRES ◽  
Greg M. DE PLATER ◽  
Magnus DOVERSKOG ◽  
Liesl C. BIRINYI-STRACHAN ◽  
Graham M. NICHOLSON ◽  
...  
Keyword(s):  
Tertiary Structure ◽  
Sequence Similarity ◽  
Three Dimensional ◽  
Amino Acid Sequences ◽  
Dimensional Structure ◽  
High Sequence Similarity ◽  
Natural Function ◽  
Global Fold ◽  
Key Residues ◽  
Β Sheet

The venom of the male Australian duck-billed platypus contains a family of four polypeptides of appox. 5 kDa, which are referred to as defensin-like peptides (DLPs). They are unique in that their amino acid sequences have no significant similarities to those of any known peptides; however, the tertiary structure of one of them, DLP-1, has recently been shown to be similar to β-defensin-12 and to the sodium neurotoxin peptide ShI (Stichodactyla helianthus neurotoxin I). Although DLPs are the major peptides in the platypus venom, little is known about their biological roles. In this study, we determined the three-dimensional structure of DLP-2 by NMR spectroscopy, with the aim of gaining insights into the natural function of the DLPs in platypus venom. The DLP-2 structure was found to incorporate a short helix that spans residues 9-12, and an antiparallel β-sheet defined by residues 15-18 and 37-40. The overall fold and cysteine-pairing pattern of DLP-2 were found to be similar to those of DLP-1, and hence β-defensin-12; however, the sequence similarities between the three molecules are relatively small. The distinct structural fold of the DLP-1, DLP-2, and β-defensin-12 is based upon several key residues that include six cysteines. DLP-3 and DLP-4 are also likely to be folded similarly since they have high sequence similarity with DLP-2. The DLPs, and β-defensin-12 may thus be grouped together into a class of polypeptide molecules which have a common or very similar global fold. The fact that the DLPs did not display antimicrobial, myotoxic, or cell-growth-promoting activities implies that the nature of the side chains in this group of peptides is likely to play an important role in defining the biological function(s).

scholarly journals Biosynthesis of the Tricyclic Aromatic Type II Polyketide Rishirilide: New Potential Third Ring Oxygenation after Three Cyclization Steps

2021 ◽  
Author(s):  
Ahmad Alali ◽  
Lin Zhang ◽  
Jianyu Li ◽  
Chijian Zuo ◽  
Dimah Wassouf ◽  
...  
Keyword(s):  
Sequence Similarity ◽  
Three Dimensional ◽  
Site Directed Mutagenesis ◽  
Dimensional Structure ◽  
Flavin Reductase ◽  
High Similarity ◽  
Dynamic Simulations ◽  
High Sequence Similarity ◽  
The Past ◽  
Biosynthetic Studies

AbstractRishirilides are a group of PKS II secondary metabolites produced by Streptomyces bottropensis Gö C4/4. Biosynthetic studies in the past have elucidated early and late steps of rishirilide biosynthesis. This work is aiming to solve the remaining steps in the rishirilide biosynthesis. Inactivation of the cyclase gene rslC3 in Streptomyces bottropensis resulted in an interruption of rishirilide production. Instead, accumulation of the tricyclic aromatic galvaquinones was observed. Similar results were observed after deletion of rslO4. Closer inspection into RslO4 crystal structure in addition to site-directed mutagenesis and molecular dynamic simulations revealed that RslO4 might be responsible for quinone formation on the third ring. The RslO1 three-dimensional structure shows a high similarity to FMN-dependent luciferase-like monooxygenases such as the epoxy-forming MsnO8 which acts with the flavin reductase MsnO3 in mensacarcin biosynthesis in the same strain. The high sequence similarity between RslO2 and MsnO3 suggests that RslO2 provides RslO1 with reduced FMN to form an epoxide that serves as substrate for RslO5.

scholarly journals BLASTing away preconceptions in crystallization trials

2019 ◽  
Vol 75 (3) ◽  
pp. 184-192 ◽  
Author(s):  
Gabriel Jan Abrahams ◽  
Janet Newman
Keyword(s):  
Protein Data Bank ◽  
Sequence Similarity ◽  
Three Dimensional ◽  
Protein Sequences ◽  
Protein Molecule ◽  
Data Bank ◽  
Dimensional Structure ◽  
Critical Step ◽  
Quantitative Verification ◽  
Better Than

Crystallization is in many cases a critical step for solving the three-dimensional structure of a protein molecule. Determining which set of chemicals to use in the initial screen is typically agnostic of the protein under investigation; however, crystallization efficiency could potentially be improved if this were not the case. Previous work has assumed that sequence similarity may provide useful information about appropriate crystallization cocktails; however, the authors are not aware of any quantitative verification of this assumption. This research investigates whether, given current information, one can detect any correlation between sequence similarity and crystallization cocktails. BLAST was used to quantitate the similarity between protein sequences in the Protein Data Bank, and this was compared with three estimations of the chemical similarities of the respective crystallization cocktails. No correlation was detected between proteins of similar (but not identical) sequence and their crystallization cocktails, suggesting that methods of determining screens based on this assumption are unlikely to result in screens that are better than those currently in use.

Zona Pellucida Proteins, Fibrils, and Matrix

2020 ◽  
Vol 89 (1) ◽  
pp. 695-715
Author(s):  
Eveline S. Litscher ◽  
Paul M. Wassarman
Keyword(s):  
Extracellular Matrix ◽  
Zona Pellucida ◽  
Three Dimensional ◽  
Structural Features ◽  
Biological Properties ◽  
Preimplantation Development ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
Early Embryos ◽  
N Terminus

The zona pellucida (ZP) is an extracellular matrix that surrounds all mammalian oocytes, eggs, and early embryos and plays vital roles during oogenesis, fertilization, and preimplantation development. The ZP is composed of three or four glycosylated proteins, ZP1–4, that are synthesized, processed, secreted, and assembled into long, cross-linked fibrils by growing oocytes. ZP proteins have an immunoglobulin-like three-dimensional structure and a ZP domain that consists of two subdomains, ZP-N and ZP-C, with ZP-N of ZP2 and ZP3 required for fibril assembly. A ZP2–ZP3 dimer is located periodically along ZP fibrils that are cross-linked by ZP1, a protein with a proline-rich N terminus. Fibrils in the inner and outer regions of the ZP are oriented perpendicular and parallel to the oolemma, respectively, giving the ZP a multilayered appearance. Upon fertilization of eggs, modification of ZP2 and ZP3 results in changes in the ZP's physical and biological properties that have important consequences. Certain structural features of ZP proteins suggest that they may be amyloid-like proteins.

scholarly journals Insights into the molecular basis of sperm–egg recognition in mammals

Reproduction ◽  
2004 ◽  
Vol 127 (4) ◽  
pp. 417-422 ◽  
Author(s):  
Tanya Hoodbhoy ◽  
Jurrien Dean
Keyword(s):  
Zona Pellucida ◽  
Three Dimensional ◽  
Explanatory Models ◽  
Dimensional Structure ◽  
Side Chain ◽  
Egg Recognition ◽  
Three Dimensional Structure ◽  
Sperm Binding ◽  
Single Protein

The zona pellucida surrounding the egg and pre-implantation embryo is required for in vivo fertility and early development. Explanatory models of sperm–egg recognition need to take into account the ability of sperm to bind to ovulated eggs, but not to two-cell embryos. For the last two decades, investigators have sought to identify an individual protein or carbohydrate side chain as the ‘sperm receptor’. However, recent genetic data in mice are more consistent with the three-dimensional structure of the zona pellucida, rather than a single protein (or carbohydrate), determining sperm binding. The mouse and human zonae pellucidae contain three glycoproteins (ZP1, ZP2, ZP3) and, following fertilization, ZP2 is proteolytically cleaved. The replacement of endogenous mouse proteins with human ZP2, ZP3 or both does not alter taxon specificity of sperm binding or prevent fertility. Surprisingly, human ZP2 is not cleaved following fertilization and intact ZP2 correlates with persistent sperm binding to two-cell embryos. Taken together, these data support a model in which the cleavage status of ZP2 modulates the three-dimensional structure of the zona pellucida and determines whether sperm bind (uncleaved) or do not (cleaved).

scholarly journals Architecturally complex O-glycopeptidases are customized for mucin recognition and hydrolysis

2021 ◽  
Vol 118 (10) ◽  
pp. e2019220118
Author(s):  
Benjamin Pluvinage ◽  
Elizabeth Ficko-Blean ◽  
Ilit Noach ◽  
Christopher Stuart ◽  
Nicole Thompson ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Peptide Bond ◽  
Molecular Organization ◽  
Dimensional Structure ◽  
Carbohydrate Binding ◽  
Functional Roles ◽  
Protein Substrates ◽  
Individual Domain ◽  
Insight Into

A challenge faced by peptidases is the recognition of highly diverse substrates. A feature of some peptidase families is the capacity to specifically use post-translationally added glycans present on their protein substrates as a recognition determinant. This is ultimately critical to enabling peptide bond hydrolysis. This class of enzyme is also frequently large and architecturally sophisticated. However, the molecular details underpinning glycan recognition by these O-glycopeptidases, the importance of these interactions, and the functional roles of their ancillary domains remain unclear. Here, using the Clostridium perfringens ZmpA, ZmpB, and ZmpC M60 peptidases as model proteins, we provide structural and functional insight into how these intricate proteins recognize glycans as part of catalytic and noncatalytic substrate recognition. Structural, kinetic, and mutagenic analyses support the key role of glycan recognition within the M60 domain catalytic site, though they point to ZmpA as an apparently inactive enzyme. Wider examination of the Zmp domain content reveals noncatalytic carbohydrate binding as a feature of these proteins. The complete three-dimensional structure of ZmpB provides rare insight into the overall molecular organization of a highly multimodular enzyme and reveals how the interplay of individual domain function may influence biological activity. O-glycopeptidases frequently occur in host-adapted microbes that inhabit or attack mucus layers. Therefore, we anticipate that these results will be fundamental to informing more detailed models of how the glycoproteins that are abundant in mucus are destroyed as part of pathogenic processes or liberated as energy sources during normal commensal lifestyles.

scholarly journals Characterization of Novel Erwinia amylovora Jumbo Bacteriophages from Eneladusvirus Genus

Viruses ◽  
2020 ◽  
Vol 12 (12) ◽  
pp. 1373
Author(s):  
Sang Guen Kim ◽  
Sung Bin Lee ◽  
Sib Sankar Giri ◽  
Hyoun Joong Kim ◽  
Sang Wha Kim ◽  
...  
Keyword(s):  
Genome Size ◽  
Sequence Similarity ◽  
Phylogenetic Analyses ◽  
Gc Content ◽  
Genomic Analysis ◽  
Open Reading Frames ◽  
Comparative Genomic ◽  
Limited Information ◽  
High Sequence Similarity ◽  
A Genome

Jumbo phages, which have a genome size of more than 200 kb, have recently been reported for the first time. However, limited information is available regarding their characteristics because few jumbo phages have been isolated. Therefore, in this study, we aimed to isolate and characterize other jumbo phages. We performed comparative genomic analysis of three Erwinia phages (pEa_SNUABM_12, pEa_SNUABM_47, and pEa_SNUABM_50), each of which had a genome size of approximately 360 kb (32.5% GC content). These phages were predicted to harbor 546, 540, and 540 open reading frames with 32, 34, and 35 tRNAs, respectively. Almost all of the genes in these phages could not be functionally annotated but showed high sequence similarity with genes encoded in Serratia phage BF, a member of Eneladusvirus. The detailed comparative and phylogenetic analyses presented in this study contribute to our understanding of the diversity and evolution of Erwinia phage and the genus Eneladusvirus.

High diversity of fungi associated with living parts of boreal forest bryophytes

Botany ◽  
2008 ◽  
Vol 86 (11) ◽  
pp. 1326-1333 ◽  
Author(s):  
Håvard Kauserud ◽  
Cecilie Mathiesen ◽  
Mikael Ohlson
Keyword(s):  
Boreal Forest ◽  
Boreal Forests ◽  
Fungal Diversity ◽  
Sequence Similarity ◽  
Phylogenetic Analyses ◽  
High Sequence Similarity ◽  
Operational Taxonomic Units ◽  
Main Portion ◽  
Similarity Searches ◽  
Small Overlap

Bryophytes are a dominant and functionally important component of the forest floor vegetation in boreal forests, yet little is known about the fungal diversity associated with these abundant plants. Using molecular identification, we document an ecologically and phylogenetically diverse array of fungi associated with the living parts of three widespread and abundant boreal forest bryophytes, i.e., Hylocomium splendens (Hedw.) Schimp. in B.S.G., Pleurozium schreberi (Brid.) Mitt., and Polytrichum commune Hedw. From 376 cloned ITS sequences, 158 operational taxonomic units (OTUs), roughly corresponding to the number of species, were defined based on sequence similarity searches (Fasta) and phylogenetic analyses. A main portion (62.8%) of the OTUs belonged to Ascomycota, 32.0% to Basidiomycota, 3.9% to Chytridiomycota, and 1.3% to Glomeromycota. The most common orders were Helotiales (18.6%), Agaricales (11.5%), Chaetothyriales (9.6%), and Tremellales (9.0%). Frequently detected OTUs of potentially high ecologic importance included two with high sequence similarity (>99%) to the agaric Entoloma conferendum (Britzelm.) Noordel and the endophyte Lophodermium piceae (Fckl.) Hoehn., and various OTUs with affinity to the Helotian genus Hyphodiscus. Several ectomycorrhiza-forming basidiomycetes were also detected. Most OTUs (77.2%) were only detected once and a very small overlap in composition of OTUs was observed among the three bryophytes, indicating the occurrence of an immense fungal diversity associated with boreal forest bryophytes that deserves further study.

scholarly journals Familial Relationships in Hyperthermo- and Acidophilic Archaeal Viruses

2010 ◽  
Vol 84 (9) ◽  
pp. 4747-4754 ◽  
Author(s):  
Lotta Johanna Happonen ◽  
Peter Redder ◽  
Xu Peng ◽  
Laila Johanne Reigstad ◽  
David Prangishvili ◽  
...  
Keyword(s):  
Structural Organization ◽  
Hot Springs ◽  
Three Dimensional ◽  
Life Cycles ◽  
Dimensional Structure ◽  
Archaeal Virus ◽  
Archaeal Viruses ◽  
Icosahedral Virus ◽  
Host Cell Interactions

ABSTRACT Archaea often live in extreme, harsh environments such as acidic hot springs and hypersaline waters. To date, only two icosahedrally symmetric, membrane-containing archaeal viruses, SH1 and Sulfolobus turreted icosahedral virus (STIV), have been described in detail. We report the sequence and three-dimensional structure of a third such virus isolated from a hyperthermoacidophilic crenarchaeon, Sulfolobus strain G4ST-2. Characterization of this new isolate revealed it to be similar to STIV on the levels of genome and structural organization. The genome organization indicates that these two viruses have diverged from a common ancestor. Interestingly, the prominent surface turrets of the two viruses are strikingly different. By sequencing and mass spectrometry, we mapped several large insertions and deletions in the known structural proteins that could account for these differences and showed that both viruses can infect the same host. A combination of genomic and proteomic analyses revealed important new insights into the structural organization of these viruses and added to our limited knowledge of archaeal virus life cycles and host-cell interactions.

Understanding the highly efficient catalysis of prokaryotic peptide deformylases by shedding light on the determinants specifying the low activity of the human counterpart

2014 ◽  
Vol 70 (2) ◽  
pp. 242-252 ◽  
Author(s):  
Sonia Fieulaine ◽  
Michel Desmadril ◽  
Thierry Meinnel ◽  
Carmela Giglione
Keyword(s):  
Sequence Similarity ◽  
Three Dimensional ◽  
Binding Pocket ◽  
Dimensional Structure ◽  
Structural Basis ◽  
Human Counterpart ◽  
Low Activity

Peptide deformylases (PDFs), which are essential and ubiquitous enzymes involved in the removal of theN-formyl group from nascent chains, are classified into four subtypes based on the structural and sequence similarity of specific conserved domains. All PDFs share a similar three-dimensional structure, are functionally interchangeablein vivoand display similar propertiesin vitro, indicating that their molecular mechanism has been conserved during evolution. The human mitochondrial PDF is the only exception as despite its conserved fold it reveals a unique substrate-binding pocket together with an unusual kinetic behaviour. Unlike human PDF, the closely related mitochondrial PDF1As from plants have catalytic efficiencies and enzymatic parameters that are similar to those of other classes of PDFs. Here, the aim was to identify the structural basis underlying the properties of human PDF compared with all other PDFs by focusing on plant mitochondrial PDF1A. The construction of a chimaera composed of plant PDF1A with the nonrandom substitutions found in a conserved motif of its human homologue converted it into an enzyme with properties similar to the human enzyme, indicating the crucial role of these positions. The crystal structure of this human-like plant PDF revealed that substitution of two residues leads to a reduction in the volume of the ligand-binding site together with the introduction of negative charges, unravelling the origin of the weak affinity of human PDF for its substrate. In addition, the substitution of the two residues of human PDF modifies the transition state of the reaction through alteration of the network of interactions between the catalytic residues and the substrate, leading to an overall reduced reaction rate.

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