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7MY0

Sy-CrtE IPP structure

Summary for 7MY0
Entry DOI10.2210/pdb7my0/pdb
DescriptorGeranylgeranyl pyrophosphate synthase, 3-METHYLBUT-3-ENYL TRIHYDROGEN DIPHOSPHATE, GLYCEROL, ... (5 entities in total)
Functional Keywordsprenyl transferase, isopentenyl pyrophosphate, dimethylallyl pyrophosphate, cyanobacteria, terpenoids, transferase
Biological sourceSynechocystis sp. (strain PCC 6803 / Kazusa)
Total number of polymer chains2
Total formula weight67730.88
Authors
Peat, T.S.,Newman, J. (deposition date: 2021-05-19, release date: 2022-06-01, Last modification date: 2023-10-18)
Primary citationSatta, A.,Esquirol, L.,Ebert, B.E.,Newman, J.,Peat, T.S.,Plan, M.,Schenk, G.,Vickers, C.E.
Molecular characterization of cyanobacterial short-chain prenyltransferases and discovery of a novel GGPP phosphatase.
Febs J., 289:6672-6693, 2022
Cited by
PubMed Abstract: Cyanobacteria are photosynthetic prokaryotes with strong potential to be used for industrial terpenoid production. However, the key enzymes forming the principal terpenoid building blocks, called short-chain prenyltransferases (SPTs), are insufficiently characterized. Here, we examined SPTs in the model cyanobacteria Synechococcus elongatus sp. PCC 7942 and Synechocystis sp. PCC 6803. Each species has a single putative SPT (SeCrtE and SyCrtE, respectively). Sequence analysis identified these as type-II geranylgeranyl pyrophosphate synthases (GGPPSs) with high homology to GGPPSs found in the plastids of green plants and other photosynthetic organisms. In vitro analysis demonstrated that SyCrtE is multifunctional, producing geranylgeranyl pyrophosphate (GGPP; C ) primarily but also significant amounts of farnesyl pyrophosphate (FPP, C ) and geranyl pyrophosphate (GPP, C ); whereas SeCrtE appears to produce only GGPP. The crystal structures were solved to 2.02 and 1.37 Å, respectively, and the superposition of the structures against the GGPPS of Synechococcus elongatus sp. PCC 7002 yield a root mean square deviation of 0.8 Å (SeCrtE) and 1.1 Å (SyCrtE). We also discovered that SeCrtE is co-encoded in an operon with a functional GGPP phosphatase, suggesting metabolic pairing of these two activities and a putative function in tocopherol biosynthesis. This work sheds light on the activity of SPTs and terpenoid synthesis in cyanobacteria. Understanding native prenyl phosphate metabolism is an important step in developing approaches to engineering the production of different chain-length terpenoids in cyanobacteria.
PubMed: 35704353
DOI: 10.1111/febs.16556
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.37 Å)
Structure validation

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