1k30
From Proteopedia
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==Crystal Structure Analysis of Squash (Cucurbita moschata) glycerol-3-phosphate (1)-acyltransferase== | ==Crystal Structure Analysis of Squash (Cucurbita moschata) glycerol-3-phosphate (1)-acyltransferase== | ||
| - | <StructureSection load='1k30' size='340' side='right' caption='[[1k30]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='1k30' size='340' side='right'caption='[[1k30]], [[Resolution|resolution]] 1.90Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1k30]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1k30]] 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=1K30 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K30 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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=1k30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k30 OCA], [https://pdbe.org/1k30 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k30 RCSB], [https://www.ebi.ac.uk/pdbsum/1k30 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k30 ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [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]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k3/1k30_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k3/1k30_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1k30 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1k30 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | BACKGROUND: Glycerol-3-phosphate (1)-acyltransferase(G3PAT) catalyzes the incorporation of an acyl group from either acyl-acyl carrier proteins (acylACPs) or acyl-CoAs into the sn-1 position of glycerol 3-phosphate to yield 1-acylglycerol-3-phosphate. G3PATs can either be selective, preferentially using the unsaturated fatty acid, oleate (C18:1), as the acyl donor, or nonselective, using either oleate or the saturated fatty acid, palmitate (C16:0), at comparable rates. The differential substrate specificity for saturated versus unsaturated fatty acids seen within this enzyme family has been implicated in the sensitivity of plants to chilling temperatures. RESULTS: The three-dimensional structure of recombinant G3PAT from squash chloroplast has been determined to 1.9 A resolution by X-ray crystallography using the technique of multiple isomorphous replacement and provides the first representative structure of an enzyme of this class. CONCLUSIONS: The tertiary structure of G3PAT comprises two domains, the larger of which, domain II, features an extensive cleft lined by hydrophobic residues and contains at one end a cluster of positively charged residues flanked by a H(X)(4)D motif, which is conserved amongst many glycerolipid acyltransferases. We predict that these hydrophobic and positively charged residues represent the binding sites for the fatty acyl substrate and the phosphate moiety of the glycerol 3-phosphate, respectively, and that the H(X)(4)D motif is a critical component of the enzyme's catalytic machinery. | ||
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| - | Analysis of the structure, substrate specificity, and mechanism of squash glycerol-3-phosphate (1)-acyltransferase.,Turnbull AP, Rafferty JB, Sedelnikova SE, Slabas AR, Schierer TP, Kroon JT, Simon JW, Fawcett T, Nishida I, Murata N, Rice DW Structure. 2001 May 9;9(5):347-53. PMID:11377195<ref>PMID:11377195</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1k30" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Cucurbita moschata]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Fawcett | + | [[Category: Fawcett T]] |
| - | [[Category: Kroon | + | [[Category: Kroon JT]] |
| - | [[Category: Murata | + | [[Category: Murata N]] |
| - | [[Category: Nishida | + | [[Category: Nishida I]] |
| - | [[Category: Rafferty | + | [[Category: Rafferty JB]] |
| - | [[Category: Rice | + | [[Category: Rice DW]] |
| - | [[Category: Schierer | + | [[Category: Schierer TP]] |
| - | [[Category: Sedelnikova | + | [[Category: Sedelnikova SE]] |
| - | [[Category: Simon | + | [[Category: Simon JW]] |
| - | [[Category: Slabas | + | [[Category: Slabas AR]] |
| - | [[Category: Turnbull | + | [[Category: Turnbull AP]] |
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Current revision
Crystal Structure Analysis of Squash (Cucurbita moschata) glycerol-3-phosphate (1)-acyltransferase
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Categories: Cucurbita moschata | Large Structures | Fawcett T | Kroon JT | Murata N | Nishida I | Rafferty JB | Rice DW | Schierer TP | Sedelnikova SE | Simon JW | Slabas AR | Turnbull AP
