9V4J

Prenyltransferase Ord1 Wild type-FSPP

Summary for 9V4J

• Entry DOI: 10.2210/pdb9v4j/pdb
• Descriptor: prenyltransferase, SULFATE ION, 1,2-ETHANEDIOL, ... (6 entities in total)
• Functional Keywords: transferase, prenyltransferase
• Biological source: Streptomyces sp. KS84
• Total number of polymer chains: 4
• Total formula weight: 145764.60

Authors

Oshiro, T.,Uehara, S.,Ito, T.,Tanaka, Y.,Kodera, Y.,Matsui, T. (deposition date: 2025-05-23, release date: 2025-10-01)

Primary citation

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, 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

Experimental method

X-RAY DIFFRACTION (2 Å)