1gu2: Difference between revisions
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<StructureSection load='1gu2' size='340' side='right'caption='[[1gu2]], [[Resolution|resolution]] 1.19Å' scene=''> | <StructureSection load='1gu2' size='340' side='right'caption='[[1gu2]], [[Resolution|resolution]] 1.19Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1gu2]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1gu2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylophilus_w3a1 Methylophilus w3a1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GU2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GU2 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr> | </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">[[1e8e|1e8e]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1e8e|1e8e]]</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=1gu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gu2 OCA], [https://pdbe.org/1gu2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gu2 RCSB], [https://www.ebi.ac.uk/pdbsum/1gu2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gu2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
Revision as of 08:47, 28 April 2021
Crystal structure of oxidized cytochrome c from Methylophilus methylotrophusCrystal structure of oxidized cytochrome c from Methylophilus methylotrophus
Structural highlights
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 crystal structures of the oxidized and reduced forms of cytochrome c" from Methylophilus methylotrophus were solved from X-ray synchrotron data to atomic resolution. The overall fold of the molecule in the two redox states is very similar and is comparable to that of the oxygen-binding protein from the purple phototrophic bacterium Rhodobacter sphaeroides. However, significant modifications occur near the haem group, in particular the detachment from axial binding of His95 observed upon reduction as well as the adoption of different conformations of some protonatable residues that form a possible proton path from the haem pocket to the protein surface. These changes are associated with the previously well characterized redox-Bohr behaviour of this protein. Furthermore they provide a model for one of the presently proposed mechanisms of proton translocation in the much more complex protein cytochrome c oxidase. Structural evidence for a proton transfer pathway coupled with haem reduction of cytochrome c" from Methylophilus methylotrophus.,Enguita FJ, Pohl E, Turner DL, Santos H, Carrondo MA J Biol Inorg Chem. 2006 Mar;11(2):189-96. Epub 2005 Dec 10. PMID:16341897[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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