7MY1

Sy-CrtE structure with IPP, N-term His-tag

これはPDB形式変換不可エントリーです。

7MY1 の概要

• エントリーDOI: 10.2210/pdb7my1/pdb
• 分子名称: Geranylgeranyl pyrophosphate synthase, 3-METHYLBUT-3-ENYL TRIHYDROGEN DIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: prenyl transferase, isopentenyl pyrophosphate, dimethylallyl pyrophosphate, cyanobacteria, terpenoids, transferase
• 由来する生物種: Synechocystis sp. (strain PCC 6803 / Kazusa)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35086.26

構造登録者

Peat, T.S.,Newman, J. (登録日: 2021-05-19, 公開日: 2022-06-01, 最終更新日: 2023-10-18)

主引用文献

Satta, 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

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

実験手法

X-RAY DIFFRACTION (1.84 Å)