7C5F

Crystal Structure of Glyceraldehyde-3-phosphate dehydrogenase1 from Escherichia coli at 1.88 Angstrom resolution

Summary for 7C5F

• Entry DOI: 10.2210/pdb7c5f/pdb
• Descriptor: Glyceraldehyde-3-phosphate dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: ecgapdh 1, nad, oxidoreductase
• Biological source: Escherichia coli BL21(DE3)
• Total number of polymer chains: 4
• Total formula weight: 154300.36

Authors

Zhang, L.,Liu, M.R.,Yao, Y.C.,Bostrom, I.K.,Wang, Y.D.,Chen, A.Q.,Li, J.X.,Gu, S.H.,Ji, C.N. (deposition date: 2020-05-20, release date: 2020-09-23, Last modification date: 2023-11-29)

Primary citation

Zhang, L.,Liu, M.R.,Yao, Y.C.,Bostrom, I.K.,Wang, Y.D.,Chen, A.Q.,Li, J.X.,Gu, S.H.,Ji, C.N.
Characterization and structure of glyceraldehyde-3-phosphate dehydrogenase type 1 from Escherichia coli.
Acta Crystallogr.,Sect.F, 76:406-413, 2020

PubMed Abstract: Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a key enzyme in the glycolytic pathway that catalyzes the conversion of D-glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate. Here, the full-length GAPDH type 1 from Escherichia coli (EcGAPDH1) was cloned and overexpressed, and the protein was purified. Biochemical analyses found that the optimum reaction temperature and pH of EcGAPDH1 were 55°C and 10.0, respectively. The protein has a certain amount of thermostability. Crystals of EcGAPDH1 were obtained using the sitting-drop vapor-diffusion technique and X-ray diffraction data were collected to 1.88 Å resolution. Characterization of the crystals showed that they belonged to space group P422, with unit-cell parameters a = b = 89.651, c = 341.007 Å, α = β = γ = 90°. The structure of EcGAPDH1 contains four subunits, each of which includes an N-terminal NAD-binding domain and a C-terminal catalytic domain. Analysis of the NAD-bound form showed some differences between the structures of EcGAPDH1 and human GAPDH. As EcGAPDH1 shares 100% identity with GAPDH from Shigella sonnei, its structure may help in finding a drug for the treatment of shigellosis.

PubMed: 32880588
DOI: 10.1107/S2053230X20010067

Experimental method

X-RAY DIFFRACTION (1.88 Å)