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  Gene sequence and the 1.8 angstrom crystal structure of the tungsten-containing formate dehydrogenase from Desulfolvibrio gigas

Raaijmakers, H., Macieira, S., Dias, J. M., Teixeira, S., Bursakov, S., Huber, R., et al. (2002). Gene sequence and the 1.8 angstrom crystal structure of the tungsten-containing formate dehydrogenase from Desulfolvibrio gigas. Structure, 10(9), 1261-1272.

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Genre: Journal Article
Alternative Title : Structure

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 Creators:
Raaijmakers, H., Author
Macieira, S.1, Author              
Dias, J. M., Author
Teixeira, S., Author
Bursakov, S., Author
Huber, R.2, Author              
Moura, J. J. G., Author
Moura, I., Author
Romao, M. J., Author
Affiliations:
1External Organizations, ou_persistent22              
2Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565155              

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Free keywords: tungsten; selenium; formate dehydrogenase; selenocysteine; molybdopterin; iron-sulfur cluster
 Abstract: Desulfiovibrio gigas formate dehydrogenase is the first representative of a tungsten-containing enzyme from a mesophile that has been structurally characterized. It is a heterodimer of 110 and 24 kDa subunits. The large subunit, homologous to E. coli FDH-H and to D. desulfuricans nitrate reductase, harbors the W site and one [4Fe-4S] center. No small subunit ortholog containing three [4Fe-4S] clusters has been reported. The structural homology with E. coli FDH-H shows that the essential residues (SeCys158, His159, and Arg407) at the active site are conserved. The active site is accessible via a positively charged tunnel, while product release may be facilitated, for H+ by buried waters and protonable amino acids and for CO2 through a hydrophobic channel.

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Language(s): eng - English
 Dates: 2002-09
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 41691
ISI: 000178030800014
 Degree: -

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Title: Structure
  Alternative Title : Structure
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 10 (9) Sequence Number: - Start / End Page: 1261 - 1272 Identifier: ISSN: 0969-2126