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Crystal Structure of the Xanthine Oxidase-Related Aldehyde Oxido-Reductase from D. gigas
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 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.
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Cites
Kabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320
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Metadata
- Authors
- Romão, M. J., Archer, M., Moura, I., Moura, J. J. G., LeGall, J., Engh, R., Schneider, M., Hof, P., & Huber, R.
- Venue
- Science
- Published
- 1995-11-17
- Volume
- 270
- Issue
- 5239
- Pages
- 1170-1176
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2027091766
- Cited by
- 480
- References
- 1
- FWCI
- 47.52
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Crystal Structure of the Xanthine Oxidase-Related Aldehyde Oxido-Reductase from D. gigas. https://app.cochat.ai/papers/10.1126/science.270.5239.1170
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- Romão, M. J., Archer, M., Moura, I., Moura, J. J. G., LeGall, J., Engh, R., Schneider, M., Hof, P., & Huber, R. (1995). Crystal Structure of the Xanthine Oxidase-Related Aldehyde Oxido-Reductase from D. gigas. Science. https://doi.org/10.1126/science.270.5239.1170
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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