Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1WLI

L122Y mutant of FMN-binding protein from Desulfovibrio vulgaris (Miyazaki F)

Summary for 1WLI
Entry DOI10.2210/pdb1wli/pdb
Related1FLM 1WLK 1WLL
DescriptorFMN-binding protein, FLAVIN MONONUCLEOTIDE (3 entities in total)
Functional Keywordselectron transport, flavoprotein, fmn
Biological sourceDesulfovibrio vulgaris str. 'Miyazaki F'
Cellular locationCytoplasm: Q46604
Total number of polymer chains2
Total formula weight27318.85
Authors
Shibata, N.,Higuchi, Y. (deposition date: 2004-06-28, release date: 2005-07-19, Last modification date: 2023-10-25)
Primary citationKitamura, M.,Terakawa, K.,Inoue, H.,Hayashida, T.,Suto, K.,Morimoto, Y.,Yasuoka, N.,Shibata, N.,Higuchi, Y.
Determination of the role of the Carboxyl-terminal leucine-122 in FMN-binding protein by mutational and structural analysis.
J.Biochem., 141:459-468, 2007
Cited by
PubMed Abstract: Mutants of flavin mononucleotide-binding protein (FMN-bp) were made by site-directed mutagenesis to investigate the role of carboxyl-terminal Leu122 of the pairing subunit in controlling redox potentials, binding the prosthetic group, and forming the tertiary and quaternary structure. We compared the oxidation-reduction potentials, FMN-binding properties, and higher structures of wild-type FMN-bp and four mutant proteins (L122Y, L122E, L122K and L122-deleted). We found that the redox potentials were affected by mutations. Also, the affinities of L122E, L122K and L122 deletion mutant apoproteins for FMN were lower than for the wild-type apoprotein, whereas the affinity of L122Y for FMN was increased. Analytical ultracentrifugation showed that the dissociation constants for dimerization of L122E and L122K were larger than for wild-type FMN-bp, whereas the dissociation constants for L122Y and the deletion mutant were lower than for the wild type. Finally, we determined the higher structures of L122Y, L122E and L122K mutants by X-ray crystallography. Our results show that the mutation of Leu122 in FMN-bp changes midpoint potentials, dissociation constants for FMN, and dimer formation, indicating that this residue is important in the pairing subunit.
PubMed: 17261542
DOI: 10.1093/jb/mvm051
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon