1m56: Difference between revisions

Revision as of 00:38, 3 May 2008

Structure of cytochrome c oxidase from Rhodobactor sphaeroides (Wild Type)

OverviewOverview

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.

About this StructureAbout this Structure

1M56 is a Protein complex structure of sequences from Rhodobacter sphaeroides. Full crystallographic information is available from OCA.

ReferenceReference

The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides., Svensson-Ek M, Abramson J, Larsson G, Tornroth S, Brzezinski P, Iwata S, J Mol Biol. 2002 Aug 9;321(2):329-39. PMID:12144789 Page seeded by OCA on Sat May 3 00:38:42 2008

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OCA

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 [[Image:1m56.gif|left|200px]]
- {{Structure
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-}}
 '''Structure of cytochrome c oxidase from Rhodobactor sphaeroides (Wild Type)'''
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 [[Category: Svensson-Ek, M.]]
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+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 00:38:42 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:11:25 2008''