1h33

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(New page: 200px<br /> <applet load="1h33" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h33, resolution 1.75&Aring;" /> '''OXIDISED SOXAX COMP...)
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Revision as of 17:15, 29 October 2007

Image:1h33.gif

1h33, resolution 1.75Å

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OXIDISED SOXAX COMPLEX FROM RHODOVULUM SULFIDOPHILUM

Overview

Reduced inorganic sulfur compounds are utilized by many bacteria as, electron donors to photosynthetic or respiratory electron transport, chains. This metabolism is a key component of the biogeochemical sulfur, cycle. The SoxAX protein is a heterodimeric c-type cytochrome involved in, thiosulfate oxidation. The crystal structures of SoxAX from the, photosynthetic bacterium Rhodovulum sulfidophilum have been solved at 1.75, A resolution in the oxidized state and at 1.5 A resolution in the, dithionite-reduced state, providing the first structural insights into the, enzymatic oxidation of thiosulfate. The SoxAX active site contains a haem, with unprecedented cysteine persulfide (cysteine sulfane) coordination., This unusual post-translational modification is also seen in, sulfurtransferases ... [(full description)]

About this Structure

1H33 is a [Protein complex] structure of sequences from [Rhodovulum sulfidophilum] with HEC as [ligand]. Full crystallographic information is available from [OCA].

Reference

Structural basis for the oxidation of thiosulfate by a sulfur cycle enzyme., Bamford VA, Bruno S, Rasmussen T, Appia-Ayme C, Cheesman MR, Berks BC, Hemmings AM, EMBO J. 2002 Nov 1;21(21):5599-610. PMID:12411478

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