scholarly journals A conserved β‐bulge glycine residue facilitates folding and increases stability of the mouse α‐defensin cryptdin‐4

2021 ◽  
Author(s):  
Richard J. Clark ◽  
Thanh Huyen Phan ◽  
Angela Song ◽  
André J. Ouellette ◽  
Anne C. Conibear ◽  
...  
Keyword(s):  
Glycine Residue

scholarly journals Evidence for an evolutionary relationship between Vmp1 and bacterial DedA proteins

2019 ◽  
Vol 63 (1-2) ◽  
pp. 67-71 ◽  
Author(s):  
Luis-Carlos Tábara ◽  
Olivier Vincent ◽  
Ricardo Escalante
Keyword(s):  
Experimental Approach ◽  
Functional Relationship ◽  
Evolutionary Relationship ◽  
Transmembrane Proteins ◽  
Lipid Homeostasis ◽  
Molecular Function ◽  
Yeast Protein ◽  
Glycine Residue ◽  
Cellular Processes ◽  
Domain Of Unknown Function

VMP1 and DedA proteins are conserved families of transmembrane proteins in eukaryotes and prokaryotes respectively. Despite numerous reports involving these proteins in multiple cellular processes, their molecular function is still unknown. They share the domain of unknown function PF09335, suggesting a possible functional relationship between these protein families. Here we show that VMP1 from different species contain two short motifs conserved in the bacterial DedA proteins and the yeast protein Tvp38. The hallmark of one of these motifs is a glycine residue previously shown to be strictly conserved in all the DedA proteins. Substitution of this residue to leucine, glutamate or arginine in Dictyostelium Vmp1 inactivates the protein, as shown by the inability of the mutants to rescue the phenotypes associated with the lack of Vmp1 including development and lipid homeostasis. This is the first experimental approach that supports an evolutionary relationship between Vmp1 and DedA proteins and highlights the importance of the conserved glycine residue in the PF09335 domain.

scholarly journals Microlunatus soli sp. nov., isolated from soil

2010 ◽  
Vol 60 (4) ◽  
pp. 824-827 ◽  
Author(s):  
P. Kämpfer ◽  
Chiu-Chung Young ◽  
H.-J. Busse ◽  
Jiunn-Nan Chu ◽  
P. Schumann ◽  
...  
Keyword(s):  
Edible Mushroom ◽  
Diaminopimelic Acid ◽  
Rrna Gene ◽  
Biochemical Tests ◽  
Glycine Residue ◽  
Gene Sequence Analysis ◽  
Peptidoglycan Structure ◽  
Unknown Phospholipid ◽  
Type Strains ◽  
Physiological And Biochemical

A Gram-stain-positive, coccoid, non-endospore-forming actinobacterium (strain CC-12602T) was isolated from a spawn used for growing the edible mushroom Agaricus brasiliensis in the laboratory. On the basis of 16S rRNA gene sequence analysis, strain CC-12602T was shown to belong to the genus Microlunatus and was related most closely to the type strains of Microlunatus ginsengisoli (96.1 % similarity), M. phosphovorus (95.9 %), M. panaciterrae (95.8 %) and M. aurantiacus (95.5 %). The quinone system comprised menaquinone MK-9(H4) as the major component and the polyamine pattern consisted of spermidine and spermine as major compounds. The predominant polar lipids were phosphatidylglycerol and unknown phospholipid PL3. Moderate amounts of diphosphatidylglycerol, an unknown glycolipid and three unknown phospholipids and minor amounts of an unknown phospholipid and a polar lipid were detected. The peptidoglycan type was A3γ′, based on ll-2,6-diaminopimelic acid with an interpeptide bridge consisting of a single glycine residue and a second glycine residue at position 1 of the peptide subunit. Peptidoglycan structure and major fatty acids (anteiso-C15 : 0, iso-C16 : 0 and iso-C15 : 0) supported the affiliation of strain CC-12602T to the genus Microlunatus. The results of physiological and biochemical tests allowed strain CC-12602T to be differentiated phenotypically from recognized Microlunatus species. Strain CC-12602T is therefore considered to represent a novel species of the genus Microlunatus, for which the name Microlunatus soli sp. nov. is proposed. The type strain is CC-12602T (=DSM 21800T =CCM 7685T).

scholarly journals Glycine in Water Favors the Polyproline II State

Biomolecules ◽  
2020 ◽  
Vol 10 (8) ◽  
pp. 1121 ◽  
Author(s):  
Brian Andrews ◽  
Shuting Zhang ◽  
Reinhard Schweitzer-Stenner ◽  
Brigita Urbanc
Keyword(s):  
Amino Acid ◽  
Spectroscopic Data ◽  
Heavy Atom ◽  
Conformational Space ◽  
Side Chain ◽  
Amino Acid Residues ◽  
Glycine Residue ◽  
Polyproline Ii ◽  
Conformational Preferences ◽  
Central Residue

Conformational preferences of amino acid residues in water are determined by the backbone and side-chain properties. Alanine is known for its high polyproline II (pPII) propensity. The question of relative contributions of the backbone and side chain to the conformational preferences of alanine and other amino acid residues in water is not fully resolved. Because glycine lacks a heavy-atom side chain, glycine-based peptides can be used to examine to which extent the backbone properties affect the conformational space. Here, we use published spectroscopic data for the central glycine residue of cationic triglycine in water to demonstrate that its conformational space is dominated by the pPII state. We assess three commonly used molecular dynamics (MD) force fields with respect to their ability to capture the conformational preferences of the central glycine residue in triglycine. We show that pPII is the mesostate that enables the functional backbone groups of the central residue to form the most hydrogen bonds with water. Our results indicate that the pPII propensity of the central glycine in GGG is comparable to that of alanine in GAG, implying that the water-backbone hydrogen bonding is responsible for the high pPII content of these residues.

scholarly journals Molecular Modeling and Implications of a Bacillus .ALPHA.-Amylase that Acquires Enhanced Thermostability and Chelator Resistance by Deletion of an Arginine-glycine Residue

2006 ◽  
Vol 53 (3) ◽  
pp. 193-197 ◽  
Author(s):  
Tadahiro Ozawa ◽  
Kazuaki Igarashi ◽  
Katsuya Ozaki ◽  
Tohru Kobayashi ◽  
Atsuo Suzuki ◽  
...  
Keyword(s):  
Molecular Modeling ◽  
Alpha Amylase ◽  
Glycine Residue

scholarly journals Activation of Orai1 Channels by Mutation of a Conserved Glycine Residue in TM1

2011 ◽  
Vol 100 (3) ◽  
pp. 182a
Author(s):  
Shenyuan L. Zhang ◽  
Andriy V. Yeromin ◽  
Junjie Hu ◽  
Anna Amcheslavsky ◽  
Hongying Zheng ◽  
...  
Keyword(s):  
Glycine Residue

scholarly journals Dual Acylation Accounts for the Localization of α19-Giardin in the Ventral Flagellum Pair of Giardia lamblia

2009 ◽  
Vol 8 (10) ◽  
pp. 1567-1574 ◽  
Author(s):  
Mirela Šarić ◽  
Anke Vahrmann ◽  
Daniela Niebur ◽  
Verena Kluempers ◽  
Adrian B. Hehl ◽  
...  
Keyword(s):  
Giardia Lamblia ◽  
Specific Protein ◽  
Cysteine Residue ◽  
Major Protein ◽  
Lipid Modification ◽  
Wild Type ◽  
Terminal Sequence ◽  
Glycine Residue ◽  
Specific Localization ◽  
Pathogenic Parasite

ABSTRACT A Giardia-specific protein family denominated as α-giardins, represents the major protein component, besides tubulin, of the cytoskeleton of the human pathogenic parasite Giardia lamblia. One of its members, α19-giardin, carries an N-terminal sequence extension of MGCXXS, which in many proteins serves as a target for dual lipid conjugation: myristoylation at the glycine residue after removal of the methionine and palmitoylation at the cysteine residue. As the first experimental evidence of a lipid modification, we found α19-giardin to be associated with the membrane fraction of disrupted trophozoites. After heterologous coexpression of α19-giardin with giardial N-myristoyltransferase (NMT) in E scherichia coli, we found the protein in a myristoylated form. Additionally, after heterologous expression together with the palmitoyl transferase Pfa3 in Saccharomyces cerevisiae, α19-giardin associates with the membrane of the main vacuole. Immunocytochemical colocalization studies on wild-type Giardia trophozoites with tubulin provide evidence that α19-giardin exclusively localizes to the ventral pair of the giardial flagella. A mutant in which the putatively myristoylated N-terminal glycine residue was replaced by alanine lost this specific localization. Our findings suggest that the dual lipidation of α19-giardin is responsible for its specific flagellar localization.

scholarly journals 3K1130 The Role of Glycine Residue of Photoactive Yellow Protein

2002 ◽  
Vol 42 (supplement2) ◽  
pp. S181
Author(s):  
Sanae Tatsumi ◽  
Nobutaka Shimizu ◽  
Yoichi Yamazaki ◽  
Hironari Kamikubo ◽  
Yasushi Imamoto ◽  
...  
Keyword(s):  
Photoactive Yellow Protein ◽  
Glycine Residue

scholarly journals Complete Virion Assembly with Scaffolding Proteins Altered in the Ability To Perform a Critical Conformational Switch

2009 ◽  
Vol 83 (15) ◽  
pp. 7391-7396 ◽  
Author(s):  
James E. Cherwa ◽  
Bentley A. Fane
Keyword(s):  
Amino Acid ◽  
Scaffolding Proteins ◽  
Wild Type ◽  
Conformational Switch ◽  
Mutant Proteins ◽  
Virion Assembly ◽  
Glycine Residue ◽  
Atomic Structures ◽  
Dominant Lethal ◽  
Α Helix

ABSTRACT In the φX174 procapsid, 240 external scaffolding proteins form a nonquasiequivalent lattice. To achieve this arrangement, the four structurally unique subunits must undergo position-dependent conformational switches. One switch is mediated by glycine residue 61, which allows a 30° kink to form in α-helix 3 in two subunits, whereas the helix is straight in the other two subunits. No other amino acid should be able to produce a bend of this magnitude. Accordingly, all substitutions for G61 are nonviable but mutant proteins differ vis-à-vis recessive and dominant phenotypes. As previously reported, amino acid substitutions with side chains larger than valine confer dominant lethal phenotypes. Alone, these mutant proteins appear to have little or no biological activity but rather require the wild-type protein to interact with other structural proteins. Proteins with conservative substitutions for G61, serine and alanine, have now been characterized. Unlike the dominant lethal proteins, these proteins do not require wild-type subunits to interact with other viral proteins and cause assembly defects reminiscent of those conferred by the lethal dominant proteins in concert with wild-type subunits. Although atomic structures suggest that only a glycine residue can provide the proper torsion angle for assembly, mutants that can productively utilize the altered external scaffolding proteins were isolated, and the mutations were mapped to the coat and internal scaffolding proteins. Thus, the ability to isolate strains that could utilize the single mutant D protein species would not have been predicted from past structural analyses.

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