1fdo: Difference between revisions
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OXIDIZED FORM OF FORMATE DEHYDROGENASE H FROM E. COLI
OverviewOverview
Formate dehydrogenase H from Escherichia coli contains selenocysteine, (SeCys), molybdenum, two molybdopterin guanine dinucleotide (MGD), cofactors, and an Fe4S4 cluster at the active site and catalyzes the, two-electron oxidation of formate to carbon dioxide. The crystal, structures of the oxidized [Mo(VI), Fe4S4(ox)] form of formate, dehydrogenase H (with and without bound inhibitor) and the reduced, [Mo(IV), Fe4S4(red)] form have been determined, revealing a four-domain, alphabeta structure with the molybdenum directly coordinated to selenium, and both MGD cofactors. These structures suggest a reaction mechanism that, directly involves SeCys140 and His141 in proton abstraction and the, molybdenum, molybdopterin, Lys44, and the Fe4S4 cluster in electron, transfer.
About this StructureAbout this Structure
1FDO is a Single protein structure of sequence from Escherichia coli with SF4, MGD and 6MO as ligands. Active as Formate dehydrogenase, with EC number 1.2.1.2 Structure known Active Sites: FS4 and MO4. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster., Boyington JC, Gladyshev VN, Khangulov SV, Stadtman TC, Sun PD, Science. 1997 Feb 28;275(5304):1305-8. PMID:9036855
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