5e8l: Difference between revisions

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== 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>  
[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>  
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== 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.
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>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
==See Also==

Latest revision as of 12:10, 20 March 2024

Crystal structure of geranylgeranyl pyrophosphate synthase 11 from Arabidopsis thalianaCrystal structure of geranylgeranyl pyrophosphate synthase 11 from Arabidopsis thaliana

Structural highlights

5e8l 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 2.807Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1]

See Also

References

  1. ↑ Wang G, Dixon RA. Heterodimeric geranyl(geranyl)diphosphate synthase from hop (Humulus lupulus) and the evolution of monoterpene biosynthesis. Proc Natl Acad Sci U S A. 2009 Jun 16;106(24):9914-9. doi:, 10.1073/pnas.0904069106. Epub 2009 May 29. PMID:19482937 doi:http://dx.doi.org/10.1073/pnas.0904069106

5e8l, resolution 2.81Å

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OCA
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