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E. COLI FLAVODOXIN AT 2.6 ANGSTROMS RESOLUTION
OverviewOverview
In Escherichia coli, flavodoxin is the physiological electron donor for, the reductive activation of the enzymes pyruvate formate-lyase, anaerobic, ribonucleotide reductase, and B12-dependent methionine synthase. As a, basis for studies of the interactions of flavodoxin with methionine, synthase, crystal structures of orthorhombic and trigonal forms of, oxidized recombinant flavodoxin from E. coli have been determined. The, orthorhombic form (space group P2(1)2(1)2(1), a = 126.4, b = 41.10, c =, 69.15 A, with two molecules per asymmetric unit) was solved initially by, molecular replacement at a resolution of 3.0 A, using coordinates from the, structure of the flavodoxin from Synechococcus PCC 7942 (Anacystis, nidulans). Data extending to 1.8-A resolution were collected at 140 K and, the ... [(full description)]
About this StructureAbout this Structure
1AHN is a [Single protein] structure of sequence from [Escherichia coli] with CA and FMN as [ligands]. Structure known Active Site: FMN. Full crystallographic information is available from [OCA].
ReferenceReference
A flavodoxin that is required for enzyme activation: the structure of oxidized flavodoxin from Escherichia coli at 1.8 A resolution., Hoover DM, Ludwig ML, Protein Sci. 1997 Dec;6(12):2525-37. PMID:9416602
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