Summary for 3A20
| Entry DOI | 10.2210/pdb3a20/pdb |
| Related | 1FLM 1WKI 1WLK |
| Descriptor | FMN-binding protein, FLAVIN MONONUCLEOTIDE (3 entities in total) |
| Functional Keywords | beta sheet, cytoplasm, electron transport, flavoprotein, fmn, transport |
| Biological source | Desulfovibrio vulgaris str. 'Miyazaki F' |
| Cellular location | Cytoplasm: Q46604 |
| Total number of polymer chains | 2 |
| Total formula weight | 27250.87 |
| Authors | Shibata, N.,Higuchi, Y. (deposition date: 2009-04-27, release date: 2009-05-19, Last modification date: 2023-11-01) |
| Primary citation | Kitamura, 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: 17261542DOI: 10.1093/jb/mvm051 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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