1TMO

TRIMETHYLAMINE N-OXIDE REDUCTASE FROM SHEWANELLA MASSILIA

1TMO の概要

• エントリーDOI: 10.2210/pdb1tmo/pdb
• 分子名称: TRIMETHYLAMINE N-OXIDE REDUCTASE, GUANYLATE-O'-PHOSPHORIC ACID MONO-(2-AMINO-5,6-DIMERCAPTO-4-OXO-3,5,6,7,8A,9,10,10A-OCTAHYDRO-4H-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-7-YLMETHYL) ESTER, MOLYBDENUM (IV)OXIDE, ... (4 entities in total)
• 機能のキーワード: oxidoreductase, tmao reductase, oxotransferase, molybdoenzyme, mo-cofactor, molybdenum, bis (molybdopterin guanine dinucleotide)
• 由来する生物種: Shewanella massilia
• 細胞内の位置: Periplasm: O87948
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 94089.94

構造登録者

Czjzek, M.,Dos Santos, J.P.,Giordano, G.,Mejean, V. (登録日: 1998-08-03, 公開日: 1999-03-30, 最終更新日: 2024-02-14)

主引用文献

Czjzek, M.,Dos Santos, J.P.,Pommier, J.,Giordano, G.,Mejean, V.,Haser, R.
Crystal structure of oxidized trimethylamine N-oxide reductase from Shewanella massilia at 2.5 A resolution.
J.Mol.Biol., 284:435-447, 1998

PubMed Abstract: 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 molybdenum coordination sphere is closest to that described in the DMSO reductase of Rhodobacter capsulatus. The structural differences found in the protein environment of the active site could be related to the differences in substrate specificity of these enzymes. In close vicinity of the molybdenum ion a tyrosine residue is missing in the TMAO reductase, leaving a greater space accessible to the solvent. This tyrosine residue has contacts to the oxo groups in the DMSO reductase structures. The arrangement and number of charged residues lining the inner surface of the funnel-like entrance to the active site, is different in the TMAO reductase than in the DMSO reductases from Rhodobacter species. Furthermore a surface loop at the top of the active-site funnel, for which no density was present in the DMSO reductase structures, is well defined in the oxidized form of the TMAO reductase structure, and is located on the border of the funnel-like entrance of the active center.

PubMed: 9813128
DOI: 10.1006/jmbi.1998.2156

実験手法

X-RAY DIFFRACTION (2.5 Å)