1e0c

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1e0c, resolution 1.8Å

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SULFURTRANSFERASE FROM AZOTOBACTER VINELANDII

Overview

Rhodanese is an ubiquitous enzyme that in vitro catalyses the transfer of, a sulfur atom from suitable donors to nucleophilic acceptors by way of a, double displacement mechanism. During the catalytic process the enzyme, cycles between a sulfur-free and a persulfide-containing form, via, formation of a persulfide linkage to a catalytic Cys residue. In the, nitrogen-fixing bacteria Azotobacter vinelandii the rhdA gene has been, identified and the encoded protein functionally characterized as a, rhodanese. The crystal structure of the A. vinelandii rhodanese has been, determined and refined at 1.8 A resolution in the sulfur-free and, persulfide-containing forms. Conservation of the overall three-dimensional, fold of bovine rhodanese is observed, with substantial modifications of, the ... [(full description)]

About this Structure

1E0C is a [Single protein] structure of sequence from [Azotobacter vinelandii] with SO4, MG and EDO as [ligands]. Active as [Thiosulfate sulfurtransferase], with EC number [2.8.1.1]. Structure known Active Site: CSS. Full crystallographic information is available from [OCA].

Reference

The crystal structure of a sulfurtransferase from Azotobacter vinelandii highlights the evolutionary relationship between the rhodanese and phosphatase enzyme families., Bordo D, Deriu D, Colnaghi R, Carpen A, Pagani S, Bolognesi M, J Mol Biol. 2000 May 12;298(4):691-704. PMID:10788330

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