3c63: Difference between revisions
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<StructureSection load='3c63' size='340' side='right'caption='[[3c63]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='3c63' size='340' side='right'caption='[[3c63]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3c63]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3c63]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C63 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C63 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
< | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3c63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c63 OCA], [https://pdbe.org/3c63 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c63 RCSB], [https://www.ebi.ac.uk/pdbsum/3c63 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c63 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3c63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c63 OCA], [https://pdbe.org/3c63 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c63 RCSB], [https://www.ebi.ac.uk/pdbsum/3c63 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c63 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/C562_ECOLX C562_ECOLX] Electron-transport protein of unknown function. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Faraone-Mennella | [[Category: Faraone-Mennella J]] | ||
[[Category: Lewis | [[Category: Lewis RA]] | ||
[[Category: Salgado | [[Category: Salgado EN]] | ||
[[Category: Tezcan | [[Category: Tezcan FA]] | ||
Latest revision as of 15:22, 30 August 2023
Tetrameric Cytochrome cb562 (K34/H59/D62/H63/H73/A74/H77) Assembly Stabilized by Interprotein Zinc CoordinationTetrameric Cytochrome cb562 (K34/H59/D62/H63/H73/A74/H77) Assembly Stabilized by Interprotein Zinc Coordination
Structural highlights
FunctionC562_ECOLX Electron-transport protein of unknown function. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe have previously demonstrated that non-self-associating protein building blocks can oligomerize to form discrete supramolecular assemblies under the control of metal coordination. We show here that secondary interactions (salt bridges and hydrogen bonds) can be critical in guiding the metal-induced self-assembly of proteins. Crystallographic and hydrodynamic measurements on appropriately engineered cytochrome cb562 variants pinpoint the importance of a single salt-bridging arginine side chain in determining whether the protein monomers form a discrete Zn-induced tetrameric complex or heterogeneous aggregates. The combined ability to direct PPIs through metal coordination and secondary interactions should provide the specificity required for the construction of complex protein superstructures and the selective control of cellular processes that involve protein-protein association reactions. Metal-mediated self-assembly of protein superstructures: influence of secondary interactions on protein oligomerization and aggregation.,Salgado EN, Lewis RA, Faraone-Mennella J, Tezcan FA J Am Chem Soc. 2008 May 14;130(19):6082-4. Epub 2008 Apr 19. PMID:18422313[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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