1f5c

CRYSTAL STRUCTURE OF F25H FERREDOXIN 1 MUTANT FROM AZOTOBACTER VINELANDII AT 1.75 ANGSTROM RESOLUTIONCRYSTAL STRUCTURE OF F25H FERREDOXIN 1 MUTANT FROM AZOTOBACTER VINELANDII AT 1.75 ANGSTROM RESOLUTION

Structural highlights 1f5c is a 1 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: , , Related: 6fdr, 7fdr, 1d3w, 1fdd Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [FER1_AZOVI] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. This ferredoxin could play a role in regulating gene expression by interacting directly with DNA. 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 Elucidating how proteins control the reduction potentials (E0') of [Fe--S] clusters is a longstanding fundamental problem in bioinorganic chemistry. Two site-directed variants of Azotobacter vinelandii ferredoxin I (FdI) that show large shifts in [Fe--S] cluster E0' (100--200 mV versus standard hydrogen electrode (SHE)) have been characterized. High resolution X-ray structures of F2H and F25H variants in their oxidized forms, and circular dichroism (CD) and electron paramagnetic resonance (EPR) of the reduced forms indicate that the overall structure is not affected by the mutations and reveal that there is no increase in solvent accessibility nor any reorientation of backbone amide dipoles or NH--S bonds. The structures, combined with detailed investigation of the variation of E0' with pH and temperature, show that the largest increases in E0' result from the introduction of positive charge due to protonation of the introduced His residues. The smaller (50--100 mV) increases observed for the neutral form are proposed to occur by directing a Hdelta+--Ndelta- dipole toward the reduced form of the cluster. Crystal structures of ferredoxin variants exhibiting large changes in [Fe-S] reduction potential.,Chen K, Bonagura CA, Tilley GJ, McEvoy JP, Jung YS, Armstrong FA, Stout CD, Burgess BK Nat Struct Biol. 2002 Mar;9(3):188-92. PMID:11875515 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ferredoxin

spinqualitylabelsall models 1f5c, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image