4IQ8

Crystal structure of glyceraldehyde-3-phosphate dehydrogenase 3 from Saccharomyces cerevisiae

Summary for 4IQ8

• Entry DOI: 10.2210/pdb4iq8/pdb
• Descriptor: Glyceraldehyde-3-phosphate dehydrogenase 3 (2 entities in total)
• Functional Keywords: rossmann fold, dehydrogenase, glyceraldehyde-3-phosphate binding, nucleus and cytoplasm, oxidoreductase
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Cellular location: Cytoplasm: P00359
• Total number of polymer chains: 1
• Total formula weight: 36808.73

Authors

Wang, H.,Liu, Q.,Niu, L.,Teng, M.,Li, X. (deposition date: 2013-01-11, release date: 2013-02-06, Last modification date: 2023-09-20)

Primary citation

Liu, Q.,Wang, H.,Liu, H.,Teng, M.,Li, X.
Preliminary crystallographic analysis of glyceraldehyde-3-phosphate dehydrogenase 3 from Saccharomyces cerevisiae.
Acta Crystallogr.,Sect.F, 68:978-980, 2012

PubMed Abstract: Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is an important enzyme in the glycolytic pathway. In addition to its conventional metabolic role, GAPDH has been identified to possess diverse cellular functions. In this study, glyceraldehyde-3-phosphate dehydrogenase 3, the third isoform of GAPDH from Saccharomyces cerevisiae, was cloned, expressed, purified and crystallized. The crystals belonged to space group I4(1)22, with unit-cell parameters a = b = 116.13, c = 119.21 Å. X-ray diffraction data were collected to a resolution of 2.6 Å. The structure was solved by molecular replacement and refinement is in progress.

PubMed: 22869137
DOI: 10.1107/S1744309112028989

Experimental method

X-RAY DIFFRACTION (2.49 Å)