1aor: Difference between revisions
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1aor ConSurf]. | ||
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Revision as of 08:31, 7 February 2016
STRUCTURE OF A HYPERTHERMOPHILIC TUNGSTOPTERIN ENZYME, ALDEHYDE FERREDOXIN OXIDOREDUCTASESTRUCTURE OF A HYPERTHERMOPHILIC TUNGSTOPTERIN ENZYME, ALDEHYDE FERREDOXIN OXIDOREDUCTASE
Structural highlights
Function[AOR_PYRFU] Catalyzes the oxidation of aldehydes to their corresponding carboxylic acids. May have a pyroglycolytic (saccharolytic) role. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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