1m56: Difference between revisions

Revision as of 23:14, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1m56.png

Template:STRUCTURE 1m56

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

Template:ABSTRACT PUBMED 12144789

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 Wed Jul 2 23:14:08 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Structure of cytochrome c oxidase from Rhodobactor sphaeroides (Wild Type)'''
+===Structure of cytochrome c oxidase from Rhodobactor sphaeroides (Wild Type)===
-==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}}
 ==About this Structure==
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 [[Category: Tornroth, S.]]
 [[Category: Membrane protein]]
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