Structure predictions and surface charge of nitrogenase flavodoxins from Klebsiella pneumoniae and Azotobacter vinelandii.
A first approximation to the tertiary structure of the nitrogenase flavodoxins of Klebsiella pneumoniae and Azotobacter vinelandii can be obtained by superimposing their amino acid sequences upon the crystallographically determined structure of the long-chain flavodoxin from Anacystis nidulans. This procedure is validated by secondary structure predictions based on the sequence alone and by the distribution of polar and hydrophobic residues. It reveals, among other things, a distinctive distribution of surface charge peculiar to the nitrogenase flavodoxins, which is probably important in determining the kinetics of electron transfer with their physiological redox partners. The most likely positions of the phosphodiester bridge which has been described in the A. vinelandii molecule can also be assessed.
D000595:Amino Acid Sequence; D001395:Azotobacter / Q000201:enzymology; D004563:Electrochemistry; D005418:Flavodoxin / Q000235:genetics; D005420:Flavoproteins / Q000235:genetics; D007711:Klebsiella pneumoniae / Q000201:enzymology; D008958:Models, Molecular; D009591:Nitrogenase / Q000378:metabolism; D010084:Oxidation-Reduction; D010710:Phosphates / Q000032:analysis; D011487:Protein Conformation; D013499:Surface Properties
D005418:Flavodoxin; D005420:Flavoproteins; D010710:Phosphates; D009591:Nitrogenase