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| [[Image:1m57.gif|left|200px]] | | {{Seed}} |
| | [[Image:1m57.png|left|200px]] |
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| {{STRUCTURE_1m57| PDB=1m57 | SCENE= }} | | {{STRUCTURE_1m57| PDB=1m57 | SCENE= }} |
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| '''Structure of cytochrome c oxidase from Rhodobacter sphaeroides (EQ(I-286) mutant))'''
| | ===Structure of cytochrome c oxidase from Rhodobacter sphaeroides (EQ(I-286) mutant))=== |
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| ==Overview==
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| The structure of cytochrome c oxidase from Rhodobacter sphaeroides has been solved at 2.3/2.8A (anisotropic resolution). This high-resolution structure revealed atomic details of a bacterial terminal oxidase including water molecule positions and a potential oxygen pathway, which has not been reported in other oxidase structures. A comparative study of the wild-type and the EQ(I-286) mutant enzyme revealed structural rearrangements around E(I-286) that could be crucial for proton transfer in this enzyme. In the structure of the mutant enzyme, EQ(I-286), which cannot transfer protons during oxygen reduction, the side-chain of Q(I-286) does not have the hydrogen bond to the carbonyl oxygen of M(I-107) that is seen in the wild-type structure. Furthermore, the Q(I-286) mutant has a different arrangement of water molecules and residues in the vicinity of the Q side-chain. These differences between the structures could reflect conformational changes that take place upon deprotonation of E(I-286) during turnover of the wild-type enzyme, which could be part of the proton-pumping machinery of the enzyme. | | The line below this paragraph, {{ABSTRACT_PUBMED_12144789}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12144789 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12144789}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Tornroth, S.]] | | [[Category: Tornroth, S.]] |
| [[Category: Membrane protein]] | | [[Category: Membrane protein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:38:51 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:14:15 2008'' |
