1dw3: Difference between revisions
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<StructureSection load='1dw3' size='340' side='right'caption='[[1dw3]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1dw3' size='340' side='right'caption='[[1dw3]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1dw3]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1dw3]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DW3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DW3 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand= | </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></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dw0|1dw0]], [[1dw1|1dw1]], [[1dw2|1dw2]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dw0|1dw0]], [[1dw1|1dw1]], [[1dw2|1dw2]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dw3 OCA], [https://pdbe.org/1dw3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dw3 RCSB], [https://www.ebi.ac.uk/pdbsum/1dw3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dw3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/SHP_RHOS4 SHP_RHOS4]] High-spin cytochrome. Transiently bind oxygen during autoxidation, which occurs with a half-life of 3 min with a 4-fold excess of O(2). Also binds carbon monoxide, azide and cyanide. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 17:48, 3 March 2021
STRUCTURE OF A REDUCED OXYGEN BINDING CYTOCHROME CSTRUCTURE OF A REDUCED OXYGEN BINDING CYTOCHROME C
Structural highlights
Function[SHP_RHOS4] High-spin cytochrome. Transiently bind oxygen during autoxidation, which occurs with a half-life of 3 min with a 4-fold excess of O(2). Also binds carbon monoxide, azide and cyanide. 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 PubMedThe photosynthetic bacterium Rhodobacter sphaeroides produces a heme protein (SHP), which is an unusual c-type cytochrome capable of transiently binding oxygen during autooxidation. Similar proteins have not only been observed in other photosynthetic bacteria but also in the obligate methylotroph Methylophilus methylotrophus and the metal reducing bacterium Shewanella putrefaciens. A three-dimensional structure of SHP was derived using the multiple isomorphous replacement phasing method. Besides a model for the oxidized state (to 1.82 A resolution), models for the reduced state (2.1 A resolution), the oxidized molecule liganded with cyanide (1. 90 A resolution), and the reduced molecule liganded with nitric oxide (2.20 A resolution) could be derived. The SHP structure represents a new variation of the class I cytochrome c fold. The oxidized state reveals a novel sixth heme ligand, Asn(88), which moves away from the iron upon reduction or when small molecules bind. The distal side of the heme has a striking resemblance to other heme proteins that bind gaseous compounds. In SHP the liberated amide group of Asn(88) stabilizes solvent-shielded ligands through a hydrogen bond. Crystal structures of an oxygen-binding cytochrome c from Rhodobacter sphaeroides.,Leys D, Backers K, Meyer TE, Hagen WR, Cusanovich MA, Van Beeumen JJ J Biol Chem. 2000 May 26;275(21):16050-6. PMID:10821858[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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