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| | <StructureSection load='1iuq' size='340' side='right'caption='[[1iuq]], [[Resolution|resolution]] 1.55Å' scene=''> | | <StructureSection load='1iuq' size='340' side='right'caption='[[1iuq]], [[Resolution|resolution]] 1.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1iuq]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1IUQ FirstGlance]. <br> | + | <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> |
| - | </td></tr><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=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55Å</td></tr> |
| - | <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> | + | <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> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glycerol-3-phosphate_1-O-acyltransferase Glycerol-3-phosphate 1-O-acyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.15 2.3.1.15] </span></td></tr>
| + | |
| | <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> | | <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> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://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.
| + | [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> |
| - | [[Category: Cucmo]] | + | [[Category: Cucurbita moschata]] |
| - | [[Category: Glycerol-3-phosphate 1-O-acyltransferase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Feese, M D]] | + | [[Category: Feese MD]] |
| - | [[Category: Kato, Y]] | + | [[Category: Kato Y]] |
| - | [[Category: Kuroki, R]] | + | [[Category: Kuroki R]] |
| - | [[Category: Tamada, T]] | + | [[Category: Tamada T]] |
| - | [[Category: Four helix bundle]]
| + | |
| - | [[Category: Open twisted alpha/beta]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
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).[1] [2] [3] [4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Stromal glycerol-3-phosphate acyltransferases (GPAT) are responsible for the selective incorporation of saturated and unsaturated fatty-acyl chains into chloroplast membranes, which is an important determinant of a plant's ability to tolerate chilling temperatures. The molecular mechanisms of plant chilling tolerance were elucidated by creating chimeric GPATs between squash (Cucurbita moscata, chilling-sensitive) and spinach (Spinacea oleracea, chilling-tolerant) and the results were interpreted using structural information on squash GPAT determined by X-ray crystallography at 1.55 A resolution. Enzymatic analysis of the chimeric GPATs showed that the chimeric GPATs containing the spinach region from residues 128 to 187 prefer the 18:1 unsaturated fatty acid rather than 16:0 saturated fatty acid. Structure analysis suggests that the size and character of the cavity that is formed from this region determines the specific recognition of acyl chains.
Substrate recognition and selectivity of plant glycerol-3-phosphate acyltransferases (GPATs) from Cucurbita moscata and Spinacea oleracea.,Tamada T, Feese MD, Ferri SR, Kato Y, Yajima R, Toguri T, Kuroki R Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):13-21. Epub 2003, Dec 18. PMID:14684887[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tamada T, Feese MD, Ferri SR, Kato Y, Yajima R, Toguri T, Kuroki R. Substrate recognition and selectivity of plant glycerol-3-phosphate acyltransferases (GPATs) from Cucurbita moscata and Spinacea oleracea. Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):13-21. Epub 2003, Dec 18. PMID:14684887
- ↑ Ferri SR, Toguri T. Substrate specificity modification of the stromal glycerol-3-phosphate acyltransferase. Arch Biochem Biophys. 1997 Jan 15;337(2):202-8. PMID:9016814 doi:10.1006/abbi.1996.9769
- ↑ Ferri SR, Toguri T. Substrate specificity modification of the stromal glycerol-3-phosphate acyltransferase. Arch Biochem Biophys. 1997 Jan 15;337(2):202-8. PMID:9016814 doi:10.1006/abbi.1996.9769
- ↑ Ferri SR, Toguri T. Substrate specificity modification of the stromal glycerol-3-phosphate acyltransferase. Arch Biochem Biophys. 1997 Jan 15;337(2):202-8. PMID:9016814 doi:10.1006/abbi.1996.9769
- ↑ Tamada T, Feese MD, Ferri SR, Kato Y, Yajima R, Toguri T, Kuroki R. Substrate recognition and selectivity of plant glycerol-3-phosphate acyltransferases (GPATs) from Cucurbita moscata and Spinacea oleracea. Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):13-21. Epub 2003, Dec 18. PMID:14684887
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