1w2l
From Proteopedia
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Revision as of 14:18, 30 October 2007
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CYTOCHROME C DOMAIN OF CAA3 OXYGEN OXIDOREDUCTASE
Overview
The cytochrome c domain of subunit II from the Rhodothermus marinus caa(3), HiPIP:oxygen oxidoreductase, a member of the superfamily of, heme-copper-containing terminal oxidases, was produced in Escherichia coli, and characterised. The recombinant protein, which shows the same optical, absorption and redox properties as the corresponding domain in the holo, enzyme, was crystallized and its structure was determined to a resolution, of 1.3 A by the multiwavelength anomalous dispersion (MAD) technique using, the anomalous dispersion of the heme iron atom. The model was refined to, final R(cryst) and R(free) values of 13.9% and 16.7%, respectively. The, structure reveals the insertion of two short antiparallel beta-strands, forming a small beta-sheet, an interesting variation of the classical ... [(full description)]
About this Structure
1W2L is a [Single protein] structure of sequence from [Rhodothermus marinus] with ACT, HEM and TRS as [ligands]. Active as [Cytochrome-c oxidase], with EC number [1.9.3.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Structure at 1.3 A resolution of Rhodothermus marinus caa(3) cytochrome c domain., Srinivasan V, Rajendran C, Sousa FL, Melo AM, Saraiva LM, Pereira MM, Santana M, Teixeira M, Michel H, J Mol Biol. 2005 Feb 4;345(5):1047-57. Epub 2004 Dec 7. PMID:15644203
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