1fvx: Difference between revisions
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Revision as of 16:08, 30 October 2007
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CLOSTRIDIUM BEIJERINCKII FLAVODOXIN MUTANT: G57N OXIDIZED
OverviewOverview
X-ray analyses of wild-type and mutant flavodoxins from Clostridium, beijerinckii show that the conformation of the peptide Gly57-Asp58, in a, bend near the isoalloxazine ring of FMN, is correlated with the oxidation, state of the FMN prosthetic group. The Gly-Asp peptide may adopt any of, three conformations: trans O-up, in which the carbonyl oxygen of Gly57, (O57) points toward the flavin ring; trans O-down, in which O57 points, away from the flavin; and cis O-down. Interconversions among these, conformers that are linked to oxidation-reduction of the flavin can, modulate the redox potentials of bound FMN. In the semiquinone and reduced, forms of the protein, the Gly57-Asp58 peptide adopts the trans O-up, conformation and accepts a hydrogen bond from the flavin N5H [Smith, W., W., ... [(full description)]
About this StructureAbout this Structure
1FVX is a [Single protein] structure of sequence from [Clostridium beijerinckii] with FMN as [ligand]. Structure known Active Site: FMN. Full crystallographic information is available from [OCA].
ReferenceReference
Control of oxidation-reduction potentials in flavodoxin from Clostridium beijerinckii: the role of conformation changes., Ludwig ML, Pattridge KA, Metzger AL, Dixon MM, Eren M, Feng Y, Swenson RP, Biochemistry. 1997 Feb 11;36(6):1259-80. PMID:9063874
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