1txg: Difference between revisions

Revision as of 16:18, 21 February 2008

Structure of glycerol-3-phosphate dehydrogenase from Archaeoglobus fulgidus

OverviewOverview

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.

About this StructureAbout this Structure

1TXG is a Single protein structure of sequence from Archaeoglobus fulgidus with , and as ligands. Active as Glycerol-3-phosphate dehydrogenase (NAD(P)(+)), with EC number 1.1.1.94 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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OCA

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-[[Image:1txg.jpg|left|200px]]<br /><applet load="1txg" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1txg.jpg|left|200px]]<br /><applet load="1txg" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1txg, resolution 1.70&Aring;" />
 '''Structure of glycerol-3-phosphate dehydrogenase from Archaeoglobus fulgidus'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-TXG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus] with SO4, NH4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glycerol-3-phosphate_dehydrogenase_(NAD(P)(+)) Glycerol-3-phosphate dehydrogenase (NAD(P)(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.94 1.1.1.94] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TXG OCA].
+TXG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=NH4:'>NH4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glycerol-3-phosphate_dehydrogenase_(NAD(P)(+)) Glycerol-3-phosphate dehydrogenase (NAD(P)(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.94 1.1.1.94] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TXG OCA].
 ==Reference==
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 [[Category: Glycerol-3-phosphate dehydrogenase (NAD(P)(+))]]
 [[Category: Single protein]]
-[[Category: Essen, L.O.]]
+[[Category: Essen, L O.]]
-[[Category: Hagemeier, C.H.]]
+[[Category: Hagemeier, C H.]]
 [[Category: Sakasegawa, S.]]
 [[Category: Shima, S.]]
-[[Category: Thauer, R.K.]]
+[[Category: Thauer, R K.]]
 [[Category: GOL]]
 [[Category: NH4]]
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 [[Category: oxidoreductase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:40:12 2007''
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