1B25

FORMALDEHYDE FERREDOXIN OXIDOREDUCTASE FROM PYROCOCCUS FURIOSUS

Summary for 1B25

• Entry DOI: 10.2210/pdb1b25/pdb
• Descriptor: PROTEIN (FORMALDEHYDE FERREDOXIN OXIDOREDUCTASE), IRON/SULFUR CLUSTER, TUNGSTOPTERIN, ... (4 entities in total)
• Functional Keywords: moco, tungstoenzyme, tungsten containing protein, hyperthermophile, oxidoreductase
• Biological source: Pyrococcus furiosus
• Total number of polymer chains: 4
• Total formula weight: 280944.87

Authors

Hu, Y.L.,Faham, S.,Roy, R.,Adams, M.W.W.,Rees, D.C. (deposition date: 1998-12-04, release date: 1999-03-24, Last modification date: 2023-08-09)

Primary citation

Hu, Y.,Faham, S.,Roy, R.,Adams, M.W.,Rees, D.C.
Formaldehyde ferredoxin oxidoreductase from Pyrococcus furiosus: the 1.85 A resolution crystal structure and its mechanistic implications.
J.Mol.Biol., 286:899-914, 1999

PubMed Abstract: Crystal structures of formaldehyde ferredoxin oxidoreductase (FOR), a tungstopterin-containing protein from the hyperthermophilic archaeon Pyrococcus furiosus, have been determined in the native state and as a complex with the inhibitor glutarate at 1.85 A and 2. 4 A resolution, respectively. The native structure was solved by molecular replacement using the structure of the homologous P. furiosus aldehyde ferredoxin oxidoreductase (AOR) as the initial model. Residues are identified in FOR that may be involved in either the catalytic mechanism or in determining substrate specificity. The binding site on FOR for the physiological electron acceptor, P. furiosus ferredoxin (Fd), has been established from an FOR-Fd cocrystal structure. Based on the arrangement of redox centers in this structure, an electron transfer pathway is proposed that begins at the tungsten center, leads to the (4Fe:4S) cluster of FOR via one of the two pterins that coordinate the tungsten, and ends at the (4Fe:4S) cluster of ferredoxin. This pathway includes two residues that coordinate the (4Fe:4S) clusters, Cys287 of FOR and Asp14 of ferredoxin. Similarities in the active site structures between FOR and the unrelated molybdoenzyme aldehyde oxidoreductase from Desulfovibrio gigas suggest that both enzymes utilize a common mechanism for aldehyde oxidation.

PubMed: 10024458
DOI: 10.1006/jmbi.1998.2488

Experimental method

X-RAY DIFFRACTION (1.85 Å)