Structure of a Hyperthermophilic Tungstopterin Enzyme, Aldehyde Ferredoxin Oxidoreductase

  • Michael K. Chan
    Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.
  • Swarnalatha Mukund
    Department of Biochemistry and Molecular Biology, and Center for Metalloenzyme Studies, University of Georgia, Athens, GA 30602, USA.
  • Arnulf Kletzin
    Department of Biochemistry and Molecular Biology, and Center for Metalloenzyme Studies, University of Georgia, Athens, GA 30602, USA.
  • Michael W. W. Adams
    Department of Biochemistry and Molecular Biology, and Center for Metalloenzyme Studies, University of Georgia, Athens, GA 30602, USA.
  • 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

  • Science

    Science 267 (5203), 1463-1469, 1995-03-10

    American Association for the Advancement of Science (AAAS)

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