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

Other Titles
Crystal structure of Bacillus subtilis glyceraldehyde-3-phosphate dehydrogenase GapB
Authors
Pawan DahalDeepak PathakEunju Kwon
Issue Date
Dec-2023
Publisher
한국구조생물학회
Citation
Biodesign, v.11, no.4, pp 59 - 65
Pages
7
Indexed
KCI
Journal Title
Biodesign
Volume
11
Number
4
Start Page
59
End Page
65
URI
https://scholarworks.gnu.ac.kr/handle/sw.gnu/69401
DOI
10.34184/kssb.2023.11.4.59
ISSN
2288-6982
2288-7105
Abstract
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+.
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자연과학대학 > Division of Life Sciences > Journal Articles

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