5e8h: Difference between revisions

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New page: '''Unreleased structure''' The entry 5e8h is ON HOLD Authors: Chengyuan Wang, Qingwen Chen, Guodong Wang, Peng Zhang Description: crystal structure of geranylfarnesyl pyrophosphate syn...
 
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'''Unreleased structure'''


The entry 5e8h is ON HOLD
==Crystal structure of geranylfarnesyl pyrophosphate synthases 2 from Arabidopsis thaliana==
<StructureSection load='5e8h' size='340' side='right'caption='[[5e8h]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5e8h]] 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=5E8H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E8H 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]] 2.3&#8491;</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=5e8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e8h OCA], [https://pdbe.org/5e8h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e8h RCSB], [https://www.ebi.ac.uk/pdbsum/5e8h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e8h ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GGPP3_ARATH GGPP3_ARATH] Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


Authors: Chengyuan Wang, Qingwen Chen, Guodong Wang, Peng Zhang
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>


Description: crystal structure of geranylfarnesyl pyrophosphate synthases 2 from Arabidopsis thaliana
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Chengyuan Wang, Qingwen Chen, Guodong Wang, Peng Zhang]]
<div class="pdbe-citations 5e8h" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Geranylgeranyl pyrophosphate synthase 3D structures|Geranylgeranyl pyrophosphate synthase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Chen Q]]
[[Category: Wang C]]
[[Category: Wang G]]
[[Category: Zhang P]]

Latest revision as of 09:17, 5 July 2023

Crystal structure of geranylfarnesyl pyrophosphate synthases 2 from Arabidopsis thalianaCrystal structure of geranylfarnesyl pyrophosphate synthases 2 from Arabidopsis thaliana

Structural highlights

5e8h is a 2 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GGPP3_ARATH Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate.

Publication Abstract from PubMed

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 (>/= 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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Wang C, Chen Q, Fan D, Li J, Wang G, Zhang P. Structural Analyses of Short-Chain Prenyltransferases Identify an Evolutionarily Conserved GFPPS Clade in Brassicaceae Plants. Mol Plant. 2016 Feb 1;9(2):195-204. doi: 10.1016/j.molp.2015.10.010. Epub 2015, Oct 30. PMID:26537048 doi:http://dx.doi.org/10.1016/j.molp.2015.10.010

5e8h, resolution 2.30Å

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