1FDI

OXIDIZED FORM OF FORMATE DEHYDROGENASE H FROM E. COLI COMPLEXED WITH THE INHIBITOR NITRITE

Summary for 1FDI

• Entry DOI: 10.2210/pdb1fdi/pdb
• Descriptor: FORMATE DEHYDROGENASE H, NITRITE ION, IRON/SULFUR CLUSTER, ... (6 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: 81440.40

Authors

Sun, P.D.,Boyington, J.C. (deposition date: 1997-01-28, 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

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: 9036855
DOI: 10.1126/science.275.5304.1305

Experimental method

X-RAY DIFFRACTION (2.9 Å)