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'''FLAVODOXIN REDUCTASE FROM E. COLI''' | '''FLAVODOXIN REDUCTASE FROM E. COLI''' | ||
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The three-dimensional structure of flavodoxin reductase from Escherichia coli at 1.7 A resolution., Ingelman M, Bianchi V, Eklund H, J Mol Biol. 1997 Apr 25;268(1):147-57. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9149148 9149148] | The three-dimensional structure of flavodoxin reductase from Escherichia coli at 1.7 A resolution., Ingelman M, Bianchi V, Eklund H, J Mol Biol. 1997 Apr 25;268(1):147-57. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9149148 9149148] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bianchi, V.]] | [[Category: Bianchi, V.]] | ||
[[Category: Eklund, H.]] | [[Category: Eklund, H.]] | ||
[[Category: Ingelman, M.]] | [[Category: Ingelman, M.]] | ||
[[Category: | [[Category: Ferredoxin reductase]] | ||
[[Category: | [[Category: Flavin]] | ||
[[Category: | [[Category: Flavodoxin reductase]] | ||
[[Category: | [[Category: Flavoprotein]] | ||
[[Category: | [[Category: Oxidoreductase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:12:42 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 16:12, 2 May 2008
FLAVODOXIN REDUCTASE FROM E. COLI
OverviewOverview
Flavodoxin reductase from Escherichia coli is an FAD-containing oxidoreductase that transports electrons between flavodoxin or ferredoxin and NADPH. Together with flavodoxin, the enzyme is involved in the reductive activation of three E. coli enzymes: cobalamin-dependent methionine synthase, pyruvate formate lyase and anaerobic ribonucleotide reductase. An additional function for the oxidoreductase appears to be to protect the bacteria against oxygen radicals. The three-dimensional structure of flavodoxin reductase has been solved by multiple isomorphous replacement, and has been refined at 1.7 A to an R-value of 18.4% and Rfree 24.8%. The monomeric molecule contains one beta-sandwich FAD domain and an alpha/beta NADP domain. The overall structure is similar to other reductases of the NADP-ferredoxin reductase family in spite of the low sequence similarities within the family. Flavodoxin reductase lacks the loop which is involved in the binding of the adenosine moiety of FAD in other FAD binding enzymes of the superfamily but is missing in the FMN binding phthalate dioxygenase reductase. Instead of this loop, the adenine interacts with an extra tryptophan at the C terminus. The FAD in flavodoxin reductase has an unusual bent conformation with a hydrogen bond between the adenine and the isoalloxazine. This is probably the cause of the unusual spectrum of the enzyme. There is a pronounced cleft close to the isoalloxazine that appears to be well suited for binding of flavodoxin/ferredoxin. Two extra short strands of the NADP-binding domain probably act as an anchor point for the binding of flavodoxin.
About this StructureAbout this Structure
1FDR is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
The three-dimensional structure of flavodoxin reductase from Escherichia coli at 1.7 A resolution., Ingelman M, Bianchi V, Eklund H, J Mol Biol. 1997 Apr 25;268(1):147-57. PMID:9149148 Page seeded by OCA on Fri May 2 16:12:42 2008