1h4i

From Proteopedia

Revision as of 13:23, 30 October 2007

METHYLOBACTERIUM EXTORQUENS METHANOL DEHYDROGENASE

Overview

BACKGROUND: Methanol dehydrogenase (MDH) is a bacterial periplasmic, quinoprotein; it has pyrrolo-quinoline quinone (PQQ) as its prosthetic, group, requires Ca2+ for activity and uses cytochrome cL as its electron, acceptor. Low-resolution structures of MDH have already been determined., RESULTS: The structure of the alpha 2 beta 2 tetramer of MDH from, Methylobacterium extorquens has now been determined at 1.94 A with an, R-factor of 19.85%. CONCLUSIONS: The alpha-subunit of MDH has an, eight-fold radial symmetry, with its eight beta-sheets stabilized by a, novel tryptophan docking motif. The PQQ in the active site is held in, place by a coplanar tryptophan and by a novel disulphide ring formed, between adjacent cysteines which are bonded by an unusual non-planar trans, peptide bond. One ... [(full description)]

About this Structure

1H4I is a [Protein complex] structure of sequences from [Methylobacterium extorquens] with CA and PQQ as [ligands]. Active as [Alcohol dehydrogenase (acceptor)], with EC number [1.1.99.8]. Structure known Active Sites: AC1, AC2, AC3 and AC4. Full crystallographic information is available from [OCA].

Reference

The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens at 1.94 A., Ghosh M, Anthony C, Harlos K, Goodwin MG, Blake C, Structure. 1995 Feb 15;3(2):177-87. PMID:7735834

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