2DUU

Crystal Structure of apo-form of NADP-Dependent Glyceraldehyde-3-Phosphate Dehydrogenase from Synechococcus Sp.

Summary for 2DUU

Entry DOI	10.2210/pdb2duu/pdb
Related	2D2I
Descriptor	Glyceraldehyde 3-phosphate dehydrogenase, SULFATE ION (3 entities in total)
Functional Keywords	glyceraldehyde 3-phosphate dehydrogenase, rossmann fold, apo-form, oxidoreductase
Biological source	Synechococcus elongatus PCC 7942
Total number of polymer chains	6
Total formula weight	248879.79
Authors	Kitatani, T.,Nakamura, Y.,Wada, K.,Kinoshita, T.,Tamoi, M.,Shigeoka, S.,Tada, T. (deposition date: 2006-07-27, release date: 2006-09-05, Last modification date: 2023-10-25)
Primary citation	Kitatani, T.,Nakamura, Y.,Wada, K.,Kinoshita, T.,Tamoi, M.,Shigeoka, S.,Tada, T. Structure of apo-glyceraldehyde-3-phosphate dehydrogenase from Synechococcus PCC7942 Acta Crystallogr.,Sect.F, 62:727-730, 2006 Cited by PubMed 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. PubMed: 16880542 DOI: 10.1107/S1744309106027916 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.9 Å)

Structure validation