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1iuq
From Proteopedia
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| - | [[Image:1iuq.png|left|200px]] | ||
| - | + | ==The 1.55 A Crystal Structure of Glycerol-3-Phosphate Acyltransferase== | |
| + | <StructureSection load='1iuq' size='340' side='right'caption='[[1iuq]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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='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='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='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> | ||
| + | == 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 == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iu/1iuq_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=1iuq ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:14684887</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1iuq" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | < | + | </StructureSection> |
[[Category: Cucurbita moschata]] | [[Category: Cucurbita moschata]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Feese | + | [[Category: Feese MD]] |
| - | [[Category: Kato | + | [[Category: Kato Y]] |
| - | [[Category: Kuroki | + | [[Category: Kuroki R]] |
| - | [[Category: Tamada | + | [[Category: Tamada T]] |
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
The 1.55 A Crystal Structure of Glycerol-3-Phosphate Acyltransferase
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