Structure of apo-glyceraldehyde-3-phosphate dehydrogenase from Synechococcus PCC7942.

ABSTRACT: 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.

SUBMITTER: Kitatani T 

PROVIDER: S-EPMC2242934 | biostudies-literature | 2006 Aug

REPOSITORIES: biostudies-literature