1tmo
From Proteopedia
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TRIMETHYLAMINE N-OXIDE REDUCTASE FROM SHEWANELLA MASSILIA
Overview
The periplasmic trimethylamine N-oxide (TMAO) reductase from the marine, bacteria Shewanella massilia is involved in a respiratory chain, having, trimethylamine N-oxide as terminal electron acceptor. This molybdoenzyme, belongs to the dimethyl sulfoxide (DMSO) reductase family, but has a, different substrate specificity than its homologous enzyme. While the DMSO, reductases reduce a broad spectra of organic S-oxide and N-oxide, compounds, TMAO reductase from Shewanella massilia reduces only TMAO as, the natural compound. The crystal structure was solved by molecular, replacement with the coordinates of the DMSO reductase from Rhodobacter, sphaeroides. The overall fold of the protein structure is essentially the, same as the DMSO reductase structures, organized into four domains. The, ... [(full description)]
About this Structure
1TMO is a [Single protein] structure of sequence from [Shewanella massilia] with 2MD and 2MO as [ligands]. Active as [[1]], with EC number [1.6.6.9]. Full crystallographic information is available from [OCA].
Reference
Crystal structure of oxidized trimethylamine N-oxide reductase from Shewanella massilia at 2.5 A resolution., Czjzek M, Dos Santos JP, Pommier J, Giordano G, Mejean V, Haser R, J Mol Biol. 1998 Nov 27;284(2):435-47. PMID:9813128
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