5e8l: Difference between revisions
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<StructureSection load='5e8l' size='340' side='right'caption='[[5e8l]], [[Resolution|resolution]] 2.81Å' scene=''> | <StructureSection load='5e8l' size='340' side='right'caption='[[5e8l]], [[Resolution|resolution]] 2.81Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5e8l]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5e8l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E8L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E8L 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]] 2.807Å</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=5e8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e8l OCA], [https://pdbe.org/5e8l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e8l RCSB], [https://www.ebi.ac.uk/pdbsum/5e8l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e8l 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/GGPP1_ARATH GGPP1_ARATH] Heterodimeric geranyl(geranyl)-diphosphate (GPP) synthase large subunit. In vitro, the large subunit catalyzes mainly the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate while the small subunit alone is inactive. Upon association of the two subunits, the product profile changes and the production of gerany-diphosphate is strongly increased.<ref>PMID:19482937</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Arabidopsis thaliana]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Chen | [[Category: Chen Q]] | ||
[[Category: Fan | [[Category: Fan D]] | ||
[[Category: Li | [[Category: Li J]] | ||
[[Category: Wang | [[Category: Wang C]] | ||
[[Category: Wang | [[Category: Wang G]] | ||
[[Category: Zhang | [[Category: Zhang P]] | ||
Revision as of 09:17, 5 July 2023
Crystal structure of geranylgeranyl pyrophosphate synthase 11 from Arabidopsis thalianaCrystal structure of geranylgeranyl pyrophosphate synthase 11 from Arabidopsis thaliana
Structural highlights
FunctionGGPP1_ARATH Heterodimeric geranyl(geranyl)-diphosphate (GPP) synthase large subunit. In vitro, the large subunit catalyzes mainly the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate while the small subunit alone is inactive. Upon association of the two subunits, the product profile changes and the production of gerany-diphosphate is strongly increased.[1] Publication Abstract from PubMedTerpenoids are the largest and most diverse class of plant-specialized metabolites, which function in diverse physiological processes during plant development. In the biosynthesis of plant terpenoids, short-chain prenyltransferases (SC-PTs), together with terpene synthases (TPSs), play critical roles in determining terpenoid diversity. SC-PTs biosynthesize prenyl pyrophosphates with different chain lengths, and these compounds are the direct precursors of terpenoids. Arabidopsis thaliana possesses a subgroup of SC-PTs whose functions are not clearly known. In this study, we focus on 10 geranylgeranyl pyrophosphate synthase-like [GGPPSL] proteins, which are commonly thought to produce GGPP [C20]. We found that a subset of members of the Arabidopsis GGPPSL gene family have undergone neo-functionalization: GGPPSL6, 7, 9, and 10 mainly have geranylfarnesyl pyrophosphate synthase activity (C25; renamed AtGFPPS1, 2, 3, and 4), and GGPPSL8 produces even longer chain prenyl pyrophosphate (>/= C30; renamed polyprenyl pyrophosphate synthase 2, AtPPPS2). By solving the crystal structures of AtGFPPS2, AtPPPS2, and AtGGPPS11, we reveal the product chain-length determination mechanism of SC-PTs and interpret it as a "three floors" model. Using this model, we identified a novel GFPPS clade distributed in Brassicaceae plants and found that the GFPPS gene typically occurs in tandem with a gene encoding a TPS, forming a GFPPS-TPS gene cluster. Structural Analyses of Short-Chain Prenyltransferases Identify an Evolutionarily Conserved GFPPS Clade in Brassicaceae Plants.,Wang C, Chen Q, Fan D, Li J, Wang G, Zhang P Mol Plant. 2016 Feb 1;9(2):195-204. doi: 10.1016/j.molp.2015.10.010. Epub 2015, Oct 30. PMID:26537048[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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