Structure of apo-glyceraldehyde-3-phosphate dehydrogenase from Synechococcus PCC7942.
The crystal structure of NADP-dependent apo-glyceraldehyde-3-phosphate dehydrogenase (apo-GAPDH) from Synechococcus PCC 7942 is reported. The crystal structure was solved by molecular replacement and refined to an R of 21.7% and R(free) of 27.5% at 2.9 angstroms resolution. The structural features of apo-GAPDH are as follows. The S-loop has an extremely flexible conformation and the sulfate ion is only taken into the classical P(i) site. A structural comparison with holo-GAPDHs indicated that the S-loop fixation is essential in the discrimination of NADP and NAD molecules.
Kitatani
Tomoya
T
Department of Applied Biochemistry, Graduate School of Agriculture and Life Sciences, Osaka Prefecture University, 1-1 Gakuen-cho, Sakai, Osaka 599-8531, Japan.
Nakamura
Yoshihiro
Y
Wada
Kei
K
Kinoshita
Takayoshi
T
Tamoi
Masahiro
M
Shigeoka
Shigeru
S
Tada
Toshiji
T
D001051:Apoenzymes / Q000737:chemistry / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry; D018360:Crystallography, X-Ray; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D009243:NAD / Q000737:chemistry / Q000378:metabolism; D009249:NADP / Q000737:chemistry / Q000378:metabolism; D017433:Protein Structure, Secondary; D013379:Substrate Specificity; D046940:Synechococcus / Q000201:enzymology*
D001051:Apoenzymes; D001426:Bacterial Proteins; D009243:NAD; D009249:NADP; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases