5e8k

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<StructureSection load='5e8k' size='340' side='right'caption='[[5e8k]], [[Resolution|resolution]] 3.03&Aring;' scene=''>
<StructureSection load='5e8k' size='340' side='right'caption='[[5e8k]], [[Resolution|resolution]] 3.03&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5e8k]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E8K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E8K FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5e8k]] 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=5E8K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E8K FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5e8h|5e8h]], [[5e8l|5e8l]]</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]] 3.028&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At3g20160, MAL21.19 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=5e8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e8k OCA], [https://pdbe.org/5e8k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e8k RCSB], [https://www.ebi.ac.uk/pdbsum/5e8k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e8k 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=5e8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e8k OCA], [http://pdbe.org/5e8k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e8k RCSB], [http://www.ebi.ac.uk/pdbsum/5e8k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e8k ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/GGPPA_ARATH GGPPA_ARATH]] Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate.
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[https://www.uniprot.org/uniprot/GGPPA_ARATH GGPPA_ARATH] Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Terpenoids 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 (&gt;/= 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.
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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<ref>PMID:26537048</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5e8k" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Geranylgeranyl pyrophosphate synthase 3D structures|Geranylgeranyl pyrophosphate synthase 3D structures]]
*[[Geranylgeranyl pyrophosphate synthase 3D structures|Geranylgeranyl pyrophosphate synthase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arath]]
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[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chen, Q]]
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[[Category: Chen Q]]
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[[Category: Fan, D]]
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[[Category: Fan D]]
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[[Category: Li, J]]
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[[Category: Li J]]
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[[Category: Wang, C]]
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[[Category: Wang C]]
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[[Category: Wang, G]]
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[[Category: Wang G]]
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[[Category: Zhang, P]]
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[[Category: Zhang P]]
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[[Category: Atppps2]]
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[[Category: Transferase]]
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Current revision

Crystal structure of polyprenyl pyrophosphate synthase 2 from Arabidopsis thaliana

PDB ID 5e8k

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