Structure of a Hyperthermophilic Tungstopterin Enzyme, Aldehyde Ferredoxin Oxidoreductase
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- Michael K. Chan
- Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.
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- Swarnalatha Mukund
- Department of Biochemistry and Molecular Biology, and Center for Metalloenzyme Studies, University of Georgia, Athens, GA 30602, USA.
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- Arnulf Kletzin
- Department of Biochemistry and Molecular Biology, and Center for Metalloenzyme Studies, University of Georgia, Athens, GA 30602, USA.
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- Michael W. W. Adams
- Department of Biochemistry and Molecular Biology, and Center for Metalloenzyme Studies, University of Georgia, Athens, GA 30602, USA.
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- Douglas C. Rees
- Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.
抄録
<jats:p> The crystal structure of the tungsten-containing aldehyde ferredoxin oxidoreductase (AOR) from <jats:italic>Pyrococcus furiosus</jats:italic> , a hyperthermophilic archaeon (formerly archaebacterium) that grows optimally at 100°C, has been determined at 2.3 angstrom resolution by means of multiple isomorphous replacement and multiple crystal form averaging. AOR consists of two identical subunits, each containing an Fe <jats:sub>4</jats:sub> S <jats:sub>4</jats:sub> cluster and a molybdopterin-based tungsten cofactor that is analogous to the molybdenum cofactor found in a large class of oxotransferases. Whereas the general features of the tungsten coordination in this cofactor were consistent with a previously proposed structure, each AOR subunit unexpectedly contained two molybdopterin molecules that coordinate a tungsten by a total of four sulfur ligands, and the pterin system was modified by an intramolecular cyclization that generated a three-ringed structure. In comparison to other proteins, the hyperthermophilic enzyme AOR has a relatively small solvent-exposed surface area, and a relatively large number of both ion pairs and buried atoms. These properties may contribute to the extreme thermostability of this enzyme. </jats:p>
収録刊行物
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- Science
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Science 267 (5203), 1463-1469, 1995-03-10
American Association for the Advancement of Science (AAAS)
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詳細情報 詳細情報について
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- CRID
- 1360011145627573888
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- NII論文ID
- 80008187206
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- ISSN
- 10959203
- 00368075
- http://id.crossref.org/issn/00368075
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