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4RGV

Crystal structure of the Methanocaldococcus jannaschii G1PDH

Summary for 4RGV
Entry DOI10.2210/pdb4rgv/pdb
Related4RFL 4RGQ
DescriptorGlycerol-1-phosphate dehydrogenase, MAGNESIUM ION, ZINC ION, ... (4 entities in total)
Functional Keywordsdehydrogenase, oxidoreductase, rossman fold, metal ion binding, nadp(h) binding, zn binding, sn-glycerol-1-phosphate dehydrogenase
Biological sourceMethanocaldococcus jannaschii
Cellular locationCytoplasm : Q58122
Total number of polymer chains2
Total formula weight82414.38
Authors
Carbone, V.,Ronimus, R.S.,Schofield, L.R.,Sutherland-Smith, A.J. (deposition date: 2014-09-30, release date: 2015-07-22, Last modification date: 2023-09-20)
Primary citationCarbone, V.,Schofield, L.R.,Zhang, Y.,Sang, C.,Dey, D.,Hannus, I.M.,Martin, W.F.,Sutherland-Smith, A.J.,Ronimus, R.S.
Structure and Evolution of the Archaeal Lipid Synthesis Enzyme sn-Glycerol-1-phosphate Dehydrogenase.
J.Biol.Chem., 290:21690-21704, 2015
Cited by
PubMed Abstract: One of the most critical events in the origins of cellular life was the development of lipid membranes. Archaea use isoprenoid chains linked via ether bonds to sn-glycerol 1-phosphate (G1P), whereas bacteria and eukaryotes use fatty acids attached via ester bonds to enantiomeric sn-glycerol 3-phosphate. NAD(P)H-dependent G1P dehydrogenase (G1PDH) forms G1P and has been proposed to have played a crucial role in the speciation of the Archaea. We present here, to our knowledge, the first structures of archaeal G1PDH from the hyperthermophilic methanogen Methanocaldococcus jannaschii with bound substrate dihydroxyacetone phosphate, product G1P, NADPH, and Zn(2+) cofactor. We also biochemically characterized the enzyme with respect to pH optimum, cation specificity, and kinetic parameters for dihydroxyacetone phosphate and NAD(P)H. The structures provide key evidence for the reaction mechanism in the stereospecific addition for the NAD(P)H-based pro-R hydrogen transfer and the coordination of the Zn(2+) cofactor during catalysis. Structure-based phylogenetic analyses also provide insight into the origins of G1PDH.
PubMed: 26175150
DOI: 10.1074/jbc.M115.647461
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.45 Å)
Structure validation

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数据于2024-10-30公开中

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