pISSN 2288-6982
eISSN 2288-7105




BioDesign 2023; 11(4): 59-65

Published online December 30, 2023

© Korean Society for Structural Biology

Crystal structure of Bacillus subtilis glyceraldehyde-3-phosphate dehydrogenase GapB

Pawan Dahal1, Deepak Pathak1 and Eunju Kwon2,3,*

1College of Pharmacy, Yeungnam University, Gyeongsan 38541, Republic of Korea
2Division of Life Science, Gyeongsang National University, Jinju 52828, Republic of Korea
3Research Institute of Molecular Alchemy, Gyeongsang National University, Jinju 52828, Republic of Korea

Correspondence to: *

Received: November 6, 2023; Revised: December 5, 2023; Accepted: December 12, 2023


Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) catalyzes the interconversion of glyceraldehyde 3-phosphate and 1,3-diphosphoglycerate during glycolysis and gluconeogenesis. In most organisms, a single GAPDH is responsible for the reaction. However, Bacillus subtilis has two isoforms of this enzyme, namely, GapA and GapB, each of which catalyzes the reaction in the opposite direction. GapA uses NAD+ as a cofactor, whereas GapB prefers NADP+. In this study, we report the crystal structure of GapB at 2.3 Å resolution. X-ray diffraction of GapB crystal was observed up to 2.0 Å resolution, and its structure was determined using molecular replacement. Its overall fold and quaternary structure (a homo-tetramer) were similar to that of the reported GAPDHs. The S-loop was missing because of the absence of the NADP+.