1FDO
OXIDIZED FORM OF FORMATE DEHYDROGENASE H FROM E. COLI
Summary for 1FDO
| Entry DOI | 10.2210/pdb1fdo/pdb |
| Descriptor | FORMATE DEHYDROGENASE H, IRON/SULFUR CLUSTER, 2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE GUANOSINE DINUCLEOTIDE, ... (5 entities in total) |
| Functional Keywords | oxidoreductase, selenium, selenocysteine, secys, molybdenum, molybdopterin, mpt, molybdopterin guanine dinucleotide, mgd, iron sulfur cluster, fe4s4, formate, dehydrogenase, anaerobic |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 81394.40 |
| Authors | Sun, P.D.,Boyington, J.C. (deposition date: 1997-01-27, release date: 1997-08-20, Last modification date: 2024-02-07) |
| Primary citation | Boyington, J.C.,Gladyshev, V.N.,Khangulov, S.V.,Stadtman, T.C.,Sun, P.D. Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster. Science, 275:1305-1308, 1997 Cited by PubMed Abstract: 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. PubMed: 9036855DOI: 10.1126/science.275.5304.1305 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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