1dgj

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1dgj, resolution 2.8Å

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CRYSTAL STRUCTURE OF THE ALDEHYDE OXIDOREDUCTASE FROM DESULFOVIBRIO DESULFURICANS ATCC 27774

Overview

The aldehyde oxidoreductase (MOD) isolated from the sulfate reducer, Desulfovibrio desulfuricans (ATCC 27774) is a member of the xanthine, oxidase family of molybdenum-containing enzymes. It has substrate, specificity similar to that of the homologous enzyme from Desulfovibrio, gigas (MOP) and the primary sequences from both enzymes show 68 %, identity. The enzyme was crystallized in space group P6(1)22, with unit, cell dimensions of a=b=156.4 A and c=177.1 A, and diffraction data were, obtained to beyond 2.8 A. The crystal structure was solved by Patterson, search techniques using the coordinates of the D. gigas enzyme. The, overall fold of the D. desulfuricans enzyme is very similar to MOP and the, few differences are mapped to exposed regions of the molecule. This is, reflected in the electrostatic potential surfaces of both homologous, enzymes, one exception being the surface potential in a region, identifiable as the putative docking site of the physiological electron, acceptor. Other essential features of the MOP structure, such as residues, of the active-site cavity, are basically conserved in MOD. Two mutations, are located in the pocket bearing a chain of catalytically relevant water, molecules.As deduced from this work, both these enzymes are very closely, related in terms of their sequences as well as 3D structures. The, comparison allowed confirmation and establishment of features that are, essential for their function; namely, conserved residues in the, active-site, catalytically relevant water molecules and recognition of the, physiological electron acceptor docking site.

About this Structure

1DGJ is a Single protein structure of sequence from Desulfovibrio desulfuricans with FES, 2MO and MCN as ligands. Full crystallographic information is available from OCA.

Reference

Gene sequence and crystal structure of the aldehyde oxidoreductase from Desulfovibrio desulfuricans ATCC 27774., Rebelo J, Macieira S, Dias JM, Huber R, Ascenso CS, Rusnak F, Moura JJ, Moura I, Romao MJ, J Mol Biol. 2000 Mar 17;297(1):135-46. PMID:10704312

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