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1iuq

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==The 1.55 A Crystal Structure of Glycerol-3-Phosphate Acyltransferase==
==The 1.55 A Crystal Structure of Glycerol-3-Phosphate Acyltransferase==
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<StructureSection load='1iuq' size='340' side='right' caption='[[1iuq]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
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<StructureSection load='1iuq' size='340' side='right'caption='[[1iuq]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1iuq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cucmo Cucmo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IUQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IUQ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1iuq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cucurbita_moschata Cucurbita moschata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IUQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IUQ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycerol-3-phosphate_1-O-acyltransferase Glycerol-3-phosphate 1-O-acyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.15 2.3.1.15] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1iuq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iuq OCA], [https://pdbe.org/1iuq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iuq RCSB], [https://www.ebi.ac.uk/pdbsum/1iuq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iuq ProSAT]</span></td></tr>
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<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=1iuq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iuq OCA], [http://pdbe.org/1iuq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1iuq RCSB], [http://www.ebi.ac.uk/pdbsum/1iuq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1iuq ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/PLSB_CUCMO PLSB_CUCMO]] Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate. The enzyme from chilling-resistant plants discriminates against non-fluid palmitic acid and selects oleic acid whereas the enzyme from sensitive plants accepts both fatty acids. Squash is chilling-sensitive.
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[https://www.uniprot.org/uniprot/GPAT2_CUCMO GPAT2_CUCMO] Esterifies the acyl-group from acyl-acyl carrier proteins (acyl-ACPs) to the sn-1 position of glycerol-3-phosphate (Ref.3). The physiological acyl donors in chloroplasts are acyl-ACPs, but acyl-CoAs are used as artificial donor for in vitro reactions (Probable). The enzyme from chilling-resistant plants discriminates against non-fluid palmitic acid and selects oleic acid whereas the enzyme from sensitive plants accepts both fatty acids (Ref.3). Squash is chilling-sensitive (Probable). Does not seem to discriminate between the acyl-ACP thioesters 18:1-ACP, 18:0-ACP and 16:0-ACP (Ref.3). Exhibits higher selectivity for 16:0-CoA than 18:1-CoA in vitro (PubMed:9016814, PubMed:14684887).<ref>PMID:14684887</ref> <ref>PMID:9016814</ref> <ref>PMID:9016814</ref> <ref>PMID:9016814</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cucmo]]
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[[Category: Cucurbita moschata]]
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[[Category: Glycerol-3-phosphate 1-O-acyltransferase]]
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[[Category: Large Structures]]
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[[Category: Feese, M D]]
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[[Category: Feese MD]]
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[[Category: Kato, Y]]
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[[Category: Kato Y]]
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[[Category: Kuroki, R]]
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[[Category: Kuroki R]]
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[[Category: Tamada, T]]
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[[Category: Tamada T]]
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[[Category: Four helix bundle]]
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[[Category: Open twisted alpha/beta]]
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[[Category: Transferase]]
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Current revision

The 1.55 A Crystal Structure of Glycerol-3-Phosphate Acyltransferase

PDB ID 1iuq

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