3atr: Difference between revisions
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==Geranylgeranyl Reductase (GGR) from Sulfolobus acidocaldarius co-crystallized with its ligand== | |||
<StructureSection load='3atr' size='340' side='right' caption='[[3atr]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3atr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33909 Atcc 33909]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ATR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ATR FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DD9:NONANE'>DD9</scene>, <scene name='pdbligand=FDA:DIHYDROFLAVINE-ADENINE+DINUCLEOTIDE'>FDA</scene>, <scene name='pdbligand=PPV:PYROPHOSPHATE'>PPV</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3atq|3atq]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Saci_0986 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2285 ATCC 33909])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3atr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3atr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3atr RCSB], [http://www.ebi.ac.uk/pdbsum/3atr PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The crystal structure of geranylgeranyl reductase (GGR) from Sulfolobus acidocaldarius was determined in order to elucidate the molecular mechanism of the catalytic reaction. The enzyme is a flavoprotein and is involved in saturation of the double bonds on the isoprenoid moiety of archaeal membranes. The structure determined in this study belongs to the p-hydroxybenzoate hydroxylase family in the glutathione reductase superfamily. GGR functions as a monomer and is divided into the FAD-binding, catalytic and C-terminal domains. The catalytic domain has a large cavity surrounded by a characteristic YxWxFPx(7-8)GxG motif and by the isoalloxazine ring of an FAD molecule. The cavity holds a lipid molecule, which is probably derived from Escherichia coli cells used for over-expression. One of the two forms of the structure clarifies the presence of an anion pocket holding a pyrophosphate molecule, which might anchor the phosphate head of the natural ligands. Mutational analysis supports the suggestion that the three aromatic residues of the YxWxFPx(7-8)GxG motif hold the ligand in the appropriate position for reduction. Cys47, which is widely conserved in GGRs, is located at the si-side of the isoalloxazine ring of FAD and is shown by mutational analysis to be involved in catalysis. The catalytic cycle, including the FAD reducing factor binding site, is proposed on the basis of the detailed analysis of the structure. | |||
Structure and mutation analysis of archaeal geranylgeranyl reductase.,Sasaki D, Fujihashi M, Iwata Y, Murakami M, Yoshimura T, Hemmi H, Miki K J Mol Biol. 2011 Jun 17;409(4):543-57. Epub 2011 Apr 16. PMID:21515284<ref>PMID:21515284</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Atcc 33909]] | [[Category: Atcc 33909]] | ||
[[Category: Fujihashi, M | [[Category: Fujihashi, M]] | ||
[[Category: Hemmi, H | [[Category: Hemmi, H]] | ||
[[Category: Iwata, Y | [[Category: Iwata, Y]] | ||
[[Category: Miki, K | [[Category: Miki, K]] | ||
[[Category: Sasaki, D | [[Category: Sasaki, D]] | ||
[[Category: Yoshimura, T | [[Category: Yoshimura, T]] | ||
[[Category: 3-di-o-geranylgeranylglyceryl phosphate]] | [[Category: 3-di-o-geranylgeranylglyceryl phosphate]] | ||
[[Category: Archaeal membrane precursor]] | [[Category: Archaeal membrane precursor]] | ||
Revision as of 01:56, 4 January 2015
Geranylgeranyl Reductase (GGR) from Sulfolobus acidocaldarius co-crystallized with its ligandGeranylgeranyl Reductase (GGR) from Sulfolobus acidocaldarius co-crystallized with its ligand
Structural highlights
Publication Abstract from PubMedThe crystal structure of geranylgeranyl reductase (GGR) from Sulfolobus acidocaldarius was determined in order to elucidate the molecular mechanism of the catalytic reaction. The enzyme is a flavoprotein and is involved in saturation of the double bonds on the isoprenoid moiety of archaeal membranes. The structure determined in this study belongs to the p-hydroxybenzoate hydroxylase family in the glutathione reductase superfamily. GGR functions as a monomer and is divided into the FAD-binding, catalytic and C-terminal domains. The catalytic domain has a large cavity surrounded by a characteristic YxWxFPx(7-8)GxG motif and by the isoalloxazine ring of an FAD molecule. The cavity holds a lipid molecule, which is probably derived from Escherichia coli cells used for over-expression. One of the two forms of the structure clarifies the presence of an anion pocket holding a pyrophosphate molecule, which might anchor the phosphate head of the natural ligands. Mutational analysis supports the suggestion that the three aromatic residues of the YxWxFPx(7-8)GxG motif hold the ligand in the appropriate position for reduction. Cys47, which is widely conserved in GGRs, is located at the si-side of the isoalloxazine ring of FAD and is shown by mutational analysis to be involved in catalysis. The catalytic cycle, including the FAD reducing factor binding site, is proposed on the basis of the detailed analysis of the structure. Structure and mutation analysis of archaeal geranylgeranyl reductase.,Sasaki D, Fujihashi M, Iwata Y, Murakami M, Yoshimura T, Hemmi H, Miki K J Mol Biol. 2011 Jun 17;409(4):543-57. Epub 2011 Apr 16. PMID:21515284[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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