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- Title
Characterization and structure of glyceraldehyde‐3‐phosphate dehydrogenase type 1 from Escherichia coli.
- 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.
- 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 P41212, 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.
- Subjects
ESCHERICHIA coli; CATALYTIC domains; GLUCOSE-6-phosphate dehydrogenase; X-ray diffraction; SPACE groups; SHIGELLA; NAD (Coenzyme)
- Publication
Acta Crystallographica: Section F, Structural Biology Communications, 2020, Vol 76, Issue 9, p406
- ISSN
2053-230X
- Publication type
Article
- DOI
10.1107/S2053230X20010067