scholarly journals Thermophilic Adaptation of Protein Complexes Inferred from Proteomic Homology Modeling

Structure ◽  
2010 ◽  
Vol 18 (7) ◽  
pp. 819-828 ◽  
Author(s):  
Bin-Guang Ma ◽  
Alexander Goncearenco ◽  
Igor N. Berezovsky
Keyword(s):  
Homology Modeling ◽  
Protein Complexes ◽  
Thermophilic Adaptation

scholarly journals Thermophilic Adaptation of Protein Complexes Inferred from Proteomic Homology Modeling

2010 ◽  
Vol 98 (3) ◽  
pp. 455a
Author(s):  
Igor N. Berezovsky ◽  
Bin-Guang Ma ◽  
Alexander Goncearenco
Keyword(s):  
Homology Modeling ◽  
Protein Complexes ◽  
Thermophilic Adaptation

Subunit Architecture of Intact Protein Complexes from Mass Spectrometry and Homology Modeling†

2008 ◽  
Vol 41 (5) ◽  
pp. 617-627 ◽  
Author(s):  
Thomas Taverner ◽  
Helena Hernández ◽  
Michal Sharon ◽  
Brandon T. Ruotolo ◽  
Dijana Matak-Vinković ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Homology Modeling ◽  
Protein Complexes ◽  
Intact Protein

ChemInform Abstract: Subunit Architecture of Intact Protein Complexes from Mass Spectrometry and Homology Modeling

ChemInform ◽  
2008 ◽  
Vol 39 (36) ◽  
Author(s):  
Thomas Taverner ◽  
Helena Hernandez ◽  
Michal Sharon ◽  
Brandon T. Ruotolo ◽  
Dijana Matak-Vinkovic ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Homology Modeling ◽  
Protein Complexes ◽  
Intact Protein

Electron Microscopy and image analysis of nucleo-protein complexes

1994 ◽  
Vol 52 ◽  
pp. 88-89
Author(s):  
E. H. Egelman ◽  
X. Yu
Keyword(s):  
Electron Microscopy ◽  
Image Analysis ◽  
Normal Cell ◽  
Genetic Recombination ◽  
Protein Complexes ◽  
Chromosomal Rearrangements ◽  
Reca Protein ◽  
E Coli ◽  
Helical Polymer ◽  
Specific Protease

The RecA protein of E. coli has been shown to mediate genetic recombination, regulate its own synthesis, control the expression of other genes, act as a specific protease, form a helical polymer and have an ATPase activity, among other observed properties. The unusual filament formed by the RecA protein on DNA has not previously been shown to exist outside of bacteria. Within this filament, the 36 Å pitch of B-form DNA is extended to about 95 Å, the pitch of the RecA helix. We have now establishedthat similar nucleo-protein complexes are formed by bacteriophage and yeast proteins, and availableevidence suggests that this structure is universal across all of biology, including humans. Thus, understanding the function of the RecA protein will reveal basic mechanisms, in existence inall organisms, that are at the foundation of general genetic recombination and repair.Recombination at this moment is assuming an importance far greater than just pure biology. The association between chromosomal rearrangements and neoplasms has become stronger and stronger, and these rearrangements are most likely products of the recombinatory apparatus of the normal cell. Further, damage to DNA appears to be a major cause of cancer.

Structure of contact sites between the outer and inner mitochondrial membranes investigated by HVEM tomography

1996 ◽  
Vol 54 ◽  
pp. 966-967
Author(s):  
C.A. Mannella ◽  
K.F. Buttle ◽  
K.A. O‘Farrell ◽  
A. Leith ◽  
M. Marko
Keyword(s):  
Liver Mitochondrion ◽  
Adenine Nucleotide ◽  
Protein Complexes ◽  
Mitochondrial Membranes ◽  
Electron Microscopic ◽  
Contact Sites ◽  
Transmission Electron ◽  
Precursor Proteins ◽  
Membrane Contacts ◽  
And Function

Early transmission electron microscopy of plastic-embedded, thin-sectioned mitochondria indicated that there are numerous junctions between the outer and inner membranes of this organelle. More recent studies have suggested that the mitochondrial membrane contacts may be the site of protein complexes engaged in specialized functions, e.g., import of mitochondrial precursor proteins, adenine nucleotide channeling, and even intermembrane signalling. It has been suggested that the intermembrane contacts may be sites of membrane fusion involving non-bilayer lipid domains in the two membranes. However, despite growing interest in the nature and function of intramitochondrial contact sites, little is known about their structure.We are using electron microscopic tomography with the Albany HVEM to determine the internal organization of mitochondria. We have reconstructed a 0.6-μm section through an isolated, plasticembedded rat-liver mitochondrion by combining 123 projections collected by tilting (+/- 70°) around two perpendicular tilt axes. The resulting 3-D image has confirmed the basic inner-membrane organization inferred from lower-resolution reconstructions obtained from single-axis tomography.

Reconstruction of Chitin-Protein Complexes Using Correlation Averaging Methods: Ovipositor of the Ichneumon Fly Megarhyssa

1980 ◽  
Vol 38 ◽  
pp. 38-39
Author(s):  
L. T. Germinario ◽  
J. Blackwell ◽  
J. Frank
Keyword(s):  
Protein Complexes ◽  
Hexagonal Lattice ◽  
Uranyl Acetate ◽  
Optical Diffraction ◽  
Insect Cuticle ◽  
High Dose ◽  
Wide Angle ◽  
X Ray ◽  
Averaging Methods ◽  
Digital Correlation

This report describes the use of digital correlation and averaging methods 1,2 for the reconstruction of high dose electron micrographs of the chitin-protein complex from Megarhyssa ovipositor. Electron microscopy of uranyl acetate stained insect cuticle has demonstrated a hexagonal array of unstained chitin monofibrils, 2.4−3.0 nm in diameter, in a stained protein matrix3,4. Optical diffraction Indicated a hexagonal lattice with a = 5.1-8.3 nm3 A particularly well ordered complex is found in the ovipositor of the ichneumon fly Megarhyssa: the small angle x-ray data gives a = 7.25 nm, and the wide angle pattern shows that the protein consists of subunits arranged in a 61 helix, with an axial repeat of 3.06 nm5.

E3 ubiquitin ligases

2005 ◽  
Vol 41 ◽  
pp. 15-30 ◽  
Author(s):  
Helen C. Ardley ◽  
Philip A. Robinson
Keyword(s):  
Protein Complexes ◽  
Loss Of Function ◽  
Direct Role ◽  
Cellular Processes ◽  
Substrate Protein ◽  
Protein Ubiquitination ◽  
C Terminus ◽  
Full Complement ◽  
Spatio Temporal ◽  
Eukaryotic Organisms

The selectivity of the ubiquitin–26 S proteasome system (UPS) for a particular substrate protein relies on the interaction between a ubiquitin-conjugating enzyme (E2, of which a cell contains relatively few) and a ubiquitin–protein ligase (E3, of which there are possibly hundreds). Post-translational modifications of the protein substrate, such as phosphorylation or hydroxylation, are often required prior to its selection. In this way, the precise spatio-temporal targeting and degradation of a given substrate can be achieved. The E3s are a large, diverse group of proteins, characterized by one of several defining motifs. These include a HECT (homologous to E6-associated protein C-terminus), RING (really interesting new gene) or U-box (a modified RING motif without the full complement of Zn2+-binding ligands) domain. Whereas HECT E3s have a direct role in catalysis during ubiquitination, RING and U-box E3s facilitate protein ubiquitination. These latter two E3 types act as adaptor-like molecules. They bring an E2 and a substrate into sufficiently close proximity to promote the substrate's ubiquitination. Although many RING-type E3s, such as MDM2 (murine double minute clone 2 oncoprotein) and c-Cbl, can apparently act alone, others are found as components of much larger multi-protein complexes, such as the anaphase-promoting complex. Taken together, these multifaceted properties and interactions enable E3s to provide a powerful, and specific, mechanism for protein clearance within all cells of eukaryotic organisms. The importance of E3s is highlighted by the number of normal cellular processes they regulate, and the number of diseases associated with their loss of function or inappropriate targeting.

Identifying redox-sensitive extra-chloroplastic enzymes by homology modeling

2000 ◽  
Vol 110 (3) ◽  
pp. 296-302
Author(s):  
Louise E. Anderson ◽  
Alex Dong Li ◽  
Elizabeth H. Muslin ◽  
Marianne Schiffer ◽  
Fred J. Stevens
Keyword(s):  
Homology Modeling

Chaperonin as the normal controls and pathological anti-stress response in the human reproductive system

2016 ◽  
pp. 126-129
Author(s):  
M. Makarenko ◽  
◽  
D. Hovsyeyev ◽  
L. Sydoryk ◽  
◽  
...  
Keyword(s):  
Reproductive System ◽  
Stress Proteins ◽  
Physiological Stress ◽  
Protein Complexes ◽  
Reproductive Function ◽  
Intercellular Signaling ◽  
Toll Like Receptors ◽  
Wide Range ◽  
Protein Functions ◽  
And Function

Different kinds of physiological stress cause mass changes in the cells, including the changes in the structure and function of the protein complexes and in separate molecules. The protein functions is determined by its folding (the spatial conclusion), which depends on the functioning of proteins of thermal shock- molecular chaperons (HSPs) or depends on the stress proteins, that are high-conservative; specialized proteins that are responsible for the correct proteinaceous folding. The family of the molecular chaperones/ chaperonins/ Hsp60 has a special place due to the its unique properties of activating the signaling cascades through the system of Toll-like receptors; it also stimulates the cells to produce anti- inflammatory cytokines, defensins, molecules of cell adhesion and the molecules of MHC; it functions as the intercellular signaling molecule. The pathological role of Hsp60 is established in a wide range of illnesses, from diabetes to atherosclerosis, where Hsp60 takes part in the regulation of both apoptosis and the autoimmune processes. The presence of the HSPs was found in different tissues that are related to the reproductive system. Key words: molecular chaperons (HSPs), Toll-like receptors, reproductive function, natural auto antibody.

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