1yob | pdb_00001yob

C69A Flavodoxin II from Azotobacter vinelandii

spinqualitylabelsall models 1yob, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1yob is a 2 chain structure with sequence from Atcc 478. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FMN, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [FLAV_AZOVI] Low-potential electron donor to a number of redox enzymes. NifF is the electron donor to nitrogenase. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Flavodoxin II from Azotobacter vinelandii is a "long-chain" flavodoxin and has one of the lowest E1 midpoint potentials found within the flavodoxin family. To better understand the relationship between structural features and redox potentials, the oxidized form of the C69A mutant of this flavodoxin was crystallized and its three-dimensional structure determined to a resolution of 2.25 A by molecular replacement. Its overall fold is similar to that of other flavodoxins, with a central five-stranded parallel beta-sheet flanked on either side by alpha-helices. An eight-residue insertion, compared with other long-chain flavodoxins, forms a short 3(10) helix preceding the start of the alpha3 helix. The flavin mononucleotide (FMN) cofactor is flanked by a leucine on its re face instead of the more conserved tryptophan, resulting in a more solvent-accessible FMN binding site and stabilization of the hydroquinone (hq) state. In particular the absence of a hydrogen bond to the N5 atom of the oxidized FMN was identified, which destabilizes the ox form, as well as an exceptionally large patch of acidic residues in the vicinity of the FMN N1 atom, which destabilizes the hq form. It is also argued that the presence of a Gly at position 58 in the sequence stabilizes the semiquinone (sq) form, as a result, raising the E2 value in particular. A crystallographic study of Cys69Ala flavodoxin II from Azotobacter vinelandii: structural determinants of redox potential.,Alagaratnam S, van Pouderoyen G, Pijning T, Dijkstra BW, Cavazzini D, Rossi GL, Van Dongen WM, van Mierlo CP, van Berkel WJ, Canters GW Protein Sci. 2005 Sep;14(9):2284-95. PMID:16131657 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Flavodoxin 3D structures

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