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Formaldehyde Ferredoxin Oxidoreductase from Pyrococcus furiosus: The 1.85 Å Resolution Crystal Structure and its Mechanistic Implications

Hu, Yonglin and Faham, Salem and Roy, Roopali and Adams, Michael W. W. and Rees, Douglas C. (1999) Formaldehyde Ferredoxin Oxidoreductase from Pyrococcus furiosus: The 1.85 Å Resolution Crystal Structure and its Mechanistic Implications. Journal of Molecular Biology, 286 (3). pp. 899-914. ISSN 0022-2836. doi:10.1006/jmbi.1998.2488. https://resolver.caltech.edu/CaltechAUTHORS:20150108-160056515

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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 Å and 2.4 Å 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.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1006/jmbi.1998.2488 DOIArticle
http://www.sciencedirect.com/science/article/pii/S0022283698924883PublisherArticle
ORCID:
AuthorORCID
Rees, Douglas C.0000-0003-4073-1185
Additional Information:© 1999 Academic Press. Received 14 September 1998; received in revised form 12 December 1998; accepted 12 December 1998. We thank Dr Michael H. B. Stowell and Dr John W. Peters for assistance with data collection. This project is supported by USPHS grants GM50775 (D.C.R.) and GM45587 (M.W.W.A.) and by the US Department of Energy grant FG05-95ER20175 (M.W.W.A.). The rotation camera facility at SSRL is supported by DOE and NIH.
Funders:
Funding AgencyGrant Number
USPHSGM50775
USPHSGM45587
Department of Energy (DOE)FG05-95ER20175
Department of Energy (DOE)UNSPECIFIED
NIHUNSPECIFIED
Subject Keywords:metalloenzymes; protein structure; tungstoenzyme; pterin; molybdenum cofactor
Issue or Number:3
DOI:10.1006/jmbi.1998.2488
Record Number:CaltechAUTHORS:20150108-160056515
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20150108-160056515
Official Citation:Yonglin Hu, Salem Faham, Roopali Roy, Michael W.W Adams, Douglas C Rees, Formaldehyde ferredoxin oxidoreductase from Pyrococcus furiosus: the 1.85 Å resolution crystal structure and its mechanistic implications, Journal of Molecular Biology, Volume 286, Issue 3, 26 February 1999, Pages 899-914, ISSN 0022-2836, http://dx.doi.org/10.1006/jmbi.1998.2488. (http://www.sciencedirect.com/science/article/pii/S0022283698924883)
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:53424
Collection:CaltechAUTHORS
Deposited By: SWORD User
Deposited On:13 Jan 2015 17:41
Last Modified:10 Nov 2021 20:01

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