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Science 17 November 1995:
Vol. 270. no. 5239, pp. 1170 - 1176
DOI: 10.1126/science.270.5239.1170
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Research Articles

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 (1)

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 a 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.


M. J. Romão and M. Archer are at the Instituto de Tecnologia Química e Biológica, Rua da Quinta Grande, 2780 Oeiras and I. S. T., Departamento Química, 1096 Lisboa Codex, Portugal. I. Moura and J. J. G. Moura are in the Departamento de Química (and CQFB) Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2825 Monte de Caparica, Portugal. J. LeGall is in the Department of Biochemistry and Molecular Biology, University of Georgia, Athens GA 30602, USA. R. Engh, M. Schneider, P. Hof, and R. Huber are at the Max-Planck-Institut für Biochemie, Am Klopferspitz, D-82152 Martinsried, Germany.
(1) To whom correspondence should be addressed.


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