1txg: Difference between revisions

Revision as of 10:18, 28 July 2008

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File:1txg.png

Template:STRUCTURE 1txg

Structure of glycerol-3-phosphate dehydrogenase from Archaeoglobus fulgidusStructure of glycerol-3-phosphate dehydrogenase from Archaeoglobus fulgidus

Template:ABSTRACT PUBMED 15557260

About this StructureAbout this Structure

1TXG is a Single protein structure of sequence from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.

ReferenceReference

Structural and functional analysis of the gpsA gene product of Archaeoglobus fulgidus: a glycerol-3-phosphate dehydrogenase with an unusual NADP+ preference., Sakasegawa S, Hagemeier CH, Thauer RK, Essen LO, Shima S, Protein Sci. 2004 Dec;13(12):3161-71. PMID:15557260

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Structure of glycerol-3-phosphate dehydrogenase from Archaeoglobus fulgidus'''
+===Structure of glycerol-3-phosphate dehydrogenase from Archaeoglobus fulgidus===
-==Overview==
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-NAD(+)-dependent glycerol-3-phosphate dehydrogenase (G3PDH) is generally absent in archaea, because archaea, unlike eukaryotes and eubacteria, utilize glycerol-1-phosphate instead of glycerol-3-phosphate for the biosynthesis of membrane lipids. Surprisingly, the genome of the hyperthermophilic archaeon Archaeoglobus fulgidus comprises a G3PDH ortholog, gpsA, most likely due to horizontal gene transfer from a eubacterial organism. Biochemical characterization proved G3PDH-like activity of the recombinant gpsA gene product. However, unlike other G3PDHs, the up to 85 degrees C thermostable A. fulgidus G3PDH exerted a 15-fold preference for NADPH over NADH. The A. fulgidus G3PDH bears the hallmarks of adaptation to halotolerance and thermophilicity, because its 1.7-A crystal structure showed a high surface density for negative charges and 10 additional intramolecular salt bridges compared to a mesophilic G3PDH structure. Whereas all amino acid residues required for dihydroxyacetone phosphate binding and reductive catalysis are highly conserved, the binding site for the adenine moiety of the NAD(P) cosubstrate shows a structural variation that reflects the observed NADPH preference, for example, by a putative salt bridge between R49 and the 2'-phosphate.
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 ==About this Structure==
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 [[Category: Thauer, R K.]]
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