4o1w
From Proteopedia
(Difference between revisions)
| (7 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of Colwellia psychrerythraea cytochrome c== | |
| + | <StructureSection load='4o1w' size='340' side='right'caption='[[4o1w]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4o1w]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Colwellia_psychrerythraea_34H Colwellia psychrerythraea 34H]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O1W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O1W FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4o1w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o1w OCA], [https://pdbe.org/4o1w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o1w RCSB], [https://www.ebi.ac.uk/pdbsum/4o1w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o1w ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q48A34_COLP3 Q48A34_COLP3] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Approximately 40% of all proteins are metalloproteins, and approximately 80% of Earth's ecosystems are at temperatures </=5 degrees C, including 90% of the global ocean. Thus, an essential aspect of marine metallobiochemistry is an understanding of the structure, dynamics, and mechanisms of cold adaptation of metalloproteins from marine microorganisms. Here, the molecular structure of the electron-transfer protein cytochrome c552 from the psychrophilic marine bacterium Colwellia psychrerythraea 34H has been determined by X-ray crystallography (PDB: ). The structure is highly superimposable with that of the homologous cytochrome from the mesophile Marinobacter hydrocarbonoclasticus. Based on structural analysis and comparison of psychrophilic, psychrotolerant, and mesophilic sequences, a methionine-based ligand-substitution mechanism for psychrophilic protein stabilization is proposed. | ||
| - | + | The structure of ferricytochrome c from the psychrophilic marine bacterium Colwellia psychrerythraea 34H.,Harvilla PB, Wolcott HN, Magyar JS Metallomics. 2014 Apr 14. PMID:24727932<ref>PMID:24727932</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4o1w" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Colwellia psychrerythraea 34H]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Harvilla PB]] | ||
| + | [[Category: Magyar JS]] | ||
| + | [[Category: Shapiro LS]] | ||
| + | [[Category: Wolcott HN]] | ||
Current revision
Crystal Structure of Colwellia psychrerythraea cytochrome c
| |||||||||||
