Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas

Maria J. Romão, Margarida Archer, Isabel Moura, José J. G. Moura, Jean LeGall, Richard Engh, Monika Schneider, Peter Hof, Robert Huber

Research output: Contribution to journalArticlepeer-review

444 Citations (Scopus)

Abstract

The crystal structure of the aldehyde oxido-reductase (Mop) from the sulfate reducing anaerobic Gram-negative bacterium Desulfovibrio gigas has been determined at 2.25 Å resolution by multiple isomorphous replacement and refined. The protein, a homodimer of 907 amino acid residues subunits, is a member of the xanthine oxidase family. The protein contains a molybdopterin cofactor (Mo-co) and two different [2Fe-2S] centers. It is folded into four domains of which the first two bind the iron sulfur centers and the last two are involved in Mo-co binding. Mo-co is a molybdenum molybdopterin cytosine dinucleotide. Molybdopterin forms a tricyclic system with the pterin bicycle annealed to pyran ring. The molybdopterin dinucleotide is deeply buried in the protein. The cis-dithiolene group of the pyran ring binds the molybdenum, which is coordinated by three more (oxygen) ligands.

Original languageEnglish
Pages (from-to)1170-1176
Number of pages7
JournalScience
Volume270
Issue number5239
Publication statusPublished - 1 Jan 1995

Fingerprint

Dive into the research topics of 'Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas'. Together they form a unique fingerprint.

Cite this