1fdo: Difference between revisions

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==Overview==
==Overview==
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.
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 Structure==
==About this Structure==
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[[Category: Formate dehydrogenase]]
[[Category: Formate dehydrogenase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Boyington, J.C.]]
[[Category: Boyington, J C.]]
[[Category: Sun, P.D.]]
[[Category: Sun, P D.]]
[[Category: 6MO]]
[[Category: 6MO]]
[[Category: MGD]]
[[Category: MGD]]
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[[Category: selenocysteine]]
[[Category: selenocysteine]]


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Revision as of 13:37, 21 February 2008

File:1fdo.jpg


1fdo, resolution 2.8Å

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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 , and as ligands. Active as Formate dehydrogenase, with EC number 1.2.1.2 Known structural/functional Sites: and . 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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