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Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase.

Chan, M. K. and Mukund, S. and Kletzin, Arnulf and Adams, M. W. and Rees, D. C. (1995):
Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase.
In: Science (New York, N.Y.), pp. 1463-9, 267, (5203), ISSN 0036-8075,
[Article]

Abstract

The crystal structure of the tungsten-containing aldehyde ferredoxin oxidoreductase (AOR) from Pyrococcus furiosus, a hyperthermophilic archaeon (formerly archaebacterium) that grows optimally at 100 degrees 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 Fe4S4 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.

Item Type: Article
Erschienen: 1995
Creators: Chan, M. K. and Mukund, S. and Kletzin, Arnulf and Adams, M. W. and Rees, D. C.
Title: Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase.
Language: English
Abstract:

The crystal structure of the tungsten-containing aldehyde ferredoxin oxidoreductase (AOR) from Pyrococcus furiosus, a hyperthermophilic archaeon (formerly archaebacterium) that grows optimally at 100 degrees 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 Fe4S4 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.

Journal or Publication Title: Science (New York, N.Y.)
Volume: 267
Number: 5203
Divisions: 10 Department of Biology > Sulfur Biochemistry and Microbial Bioenergetics
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10 Department of Biology
Date Deposited: 24 May 2011 09:28
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