1aor
STRUCTURE OF A HYPERTHERMOPHILIC TUNGSTOPTERIN ENZYME, ALDEHYDE FERREDOXIN OXIDOREDUCTASE
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OverviewOverview
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.
About this StructureAbout this Structure
1AOR is a Single protein structure of sequence from Pyrococcus furiosus with FE, NA, SF4 and PTE as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase., Chan MK, Mukund S, Kletzin A, Adams MW, Rees DC, Science. 1995 Mar 10;267(5203):1463-9. PMID:7878465
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