9V4H

Prenyltransferase Ord1 Q216A-FSPP

9V4H の概要

• エントリーDOI: 10.2210/pdb9v4h/pdb
• 分子名称: prenyltransferase, S-[(2E,6E)-3,7,11-TRIMETHYLDODECA-2,6,10-TRIENYL] TRIHYDROGEN THIODIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: transferase, prenyltransferase
• 由来する生物種: Streptomyces sp. KS84
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 145374.02

構造登録者

Oshiro, T.,Uehara, S.,Ito, T.,Tanaka, Y.,Kodera, Y.,Matsui, T. (登録日: 2025-05-23, 公開日: 2025-10-01, 最終更新日: 2025-10-22)

主引用文献

Oshiro, T.,Uehara, S.,Suto, A.,Tanaka, Y.,Ito, T.,Kodera, Y.,Matsui, T.
Structure-Activity Relationship of an All-alpha-helical Prenyltransferase Reveals the Mechanism of Indole Prenylation.
Biochemistry, 64:4196-4205, 2025

PubMed Abstract: Enzymes are involved in the biosynthesis of a variety of secondary metabolites found in nature. The catalytic mechanism is regulated by the three-dimensional structure of the enzyme, particularly at the catalytic site, resulting in the synthesis of natural products with complex conformations derived from a regioselective, chemoselective, or stereoselective preference of the enzyme reaction. Prenyltransferase, which belongs to the prenylsynthase superfamily, catalyzes the condensation of isoprene to an aromatic compound, consequently producing a terpenoid scaffold structure. Prenyltransferase thus plays an important role in expanding the chemical diversity of the terpenoids. Although the three-dimensional structures of prenylsynthases categorized in the same superfamily have been resolved, the catalytic mechanism of prenyltransferase has been veiled. In this study, we determined the X-ray crystal structure of a novel prenyltransferase, Ord1, which is derived from . Here, we report the enzymatic characteristics of the Ord1 and discuss its catalytic mechanism.

PubMed: 40968638
DOI: 10.1021/acs.biochem.5c00329

実験手法

X-RAY DIFFRACTION (2.2 Å)