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1m56

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(New page: 200px<br /><applet load="1m56" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m56, resolution 2.3&Aring;" /> '''Structure of cytochro...)
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Revision as of 19:02, 20 November 2007

Image:1m56.gif

1m56, resolution 2.3Å

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

Overview

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 Structure

1M56 is a Protein complex structure of sequences from Rhodobacter sphaeroides with CU, MG, CA, HEA and PEH as ligands. Active as Cytochrome-c oxidase, with EC number 1.9.3.1 Full crystallographic information is available from OCA.

Reference

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

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