How do the x-ray structure and the NMR structure of FMN-binding protein differ?
The crystal structure of FMN-binding protein (FMN-bp) from Desulfovibrio vulgaris Miyazaki F was solved by the multiple isomorphous replacement method and refined to an R factor of 15.1% at 1.3 A resolution. FMN-bp exists in a dimeric form in the crystal, in contrast to the monomeric structure determined by NMR. R.m.s. deviations between the crystal structure and the solution structure are more than 2 A, which implies significant differences. There are some hydrophobic residues in the interface between the two monomers. In particular, Leu122 in the C-terminus has a close contact with the o-xylene moiety of FMN, while solvent molecules may cover the o-xylene moiety in the solution structure.
Suto
K
K
Department of Life Science, Faculty of Science, Himeji Institute of Technology, 3-2-1 Kouto, Kamigori Ako-gun, Hyogo 678-1297, Japan.
Kawagoe
K
K
Shibata
N
N
Morimoto
Y
Y
Higuchi
Y
Y
Kitamura
M
M
Nakaya
T
T
Yasuoka
N
N
D001426:Bacterial Proteins / Q000737:chemistry*; D002352:Carrier Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D016969:Desulfovibrio vulgaris / Q000737:chemistry*; D019281:Dimerization; D005420:Flavoproteins; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D011487:Protein Conformation; D012997:Solvents; D014992:Xylenes
D001426:Bacterial Proteins; D002352:Carrier Proteins; C086046:FMN-binding protein, Desulfovibrio vulgaris; D005420:Flavoproteins; D012997:Solvents; D014992:Xylenes; C026114:2-xylene