PDBsum entry 3kra

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protein ligands metals Protein-protein interface(s) links
Transferase PDB id
Protein chains
279 a.a. *
259 a.a. *
_MG ×3
Waters ×1301
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Mint heterotetrameric geranyl pyrophosphate synthase in comp magnesium
Structure: Geranyl diphosphate synthase large subunit. Chain: a, d. Fragment: unp residues 84-377. Synonym: gpps large subunit, geranyl pyrophosphate synthase subunit, gpp synthase large subunit. Engineered: yes. Geranyl diphosphate synthase small subunit. Chain: b, c. Fragment: unp residues 49-313.
Source: Mentha x piperita. Peppermint. Organism_taxid: 34256. Gene: gpps large subunit. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: gpps small subunit.
1.90Å     R-factor:   0.176     R-free:   0.216
Authors: T.-H.Chang,T.-P.Ko,F.-L.Hsieh,A.H.-J.Wang
Key ref: T.H.Chang et al. (2010). Structure of a heterotetrameric geranyl pyrophosphate synthase from mint (Mentha piperita) reveals intersubunit regulation. Plant Cell, 22, 454-467. PubMed id: 20139160
18-Nov-09     Release date:   23-Feb-10    
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Protein chains
Pfam   ArchSchema ?
Q9SBR3  (Q9SBR3_MENPI) -  Geranyl diphosphate synthase large subunit
377 a.a.
279 a.a.*
Protein chains
Pfam   ArchSchema ?
Q9SBR4  (Q9SBR4_MENPI) -  Geranyl diphosphate synthase small subunit
313 a.a.
259 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     isoprenoid biosynthetic process   1 term 


Plant Cell 22:454-467 (2010)
PubMed id: 20139160  
Structure of a heterotetrameric geranyl pyrophosphate synthase from mint (Mentha piperita) reveals intersubunit regulation.
T.H.Chang, F.L.Hsieh, T.P.Ko, K.H.Teng, P.H.Liang, A.H.Wang.
Terpenes (isoprenoids), derived from isoprenyl pyrophosphates, are versatile natural compounds that act as metabolism mediators, plant volatiles, and ecological communicators. Divergent evolution of homomeric prenyltransferases (PTSs) has allowed PTSs to optimize their active-site pockets to achieve catalytic fidelity and diversity. Little is known about heteromeric PTSs, particularly the mechanisms regulating formation of specific products. Here, we report the crystal structure of the (LSU . SSU)(2)-type (LSU/SSU = large/small subunit) heterotetrameric geranyl pyrophosphate synthase (GPPS) from mint (Mentha piperita). The LSU and SSU of mint GPPS are responsible for catalysis and regulation, respectively, and this SSU lacks the essential catalytic amino acid residues found in LSU and other PTSs. Whereas no activity was detected for individually expressed LSU or SSU, the intact (LSU . SSU)(2) tetramer produced not only C(10)-GPP at the beginning of the reaction but also C(20)-GGPP (geranylgeranyl pyrophosphate) at longer reaction times. The activity for synthesizing C(10)-GPP and C(20)-GGPP, but not C(15)-farnesyl pyrophosphate, reflects a conserved active-site structure of the LSU and the closely related mustard (Sinapis alba) homodimeric GGPPS. Furthermore, using a genetic complementation system, we showed that no C(20)-GGPP is produced by the mint GPPS in vivo. Presumably through protein-protein interactions, the SSU remodels the active-site cavity of LSU for synthesizing C(10)-GPP, the precursor of volatile C(10)-monoterpenes.