Open AccessStructure of apo‐glyceraldehyde‐3‐phosphate dehydrogenase from Synechococcus PCC7942
Author(s) -
Wada Kei,
Kitatani Tomoya,
Tamoi Masahiro,
Nakamura Yoshihiro,
Kinoshita Takayoshi,
Shigeoka Shigeru,
Tada Toshiji
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106027916
Subject(s) - glyceraldehyde 3 phosphate dehydrogenase , nad+ kinase , dehydrogenase , molecular replacement , chemistry , crystal structure , biochemistry , molecule , stereochemistry , crystallography , enzyme , organic chemistry
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 Å 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.