7VEO

Crystal structure of juvenile hormone acid methyltransferase silkworm JHAMT isoform3 complex with S-Adenosyl-L-homocysteine

7VEO の概要

• エントリーDOI: 10.2210/pdb7veo/pdb
• 分子名称: Methyltranfer_dom domain-containing protein, S-ADENOSYL-L-HOMOCYSTEINE (3 entities in total)
• 機能のキーワード: juvenile hormone, methyltransferase, insects, hormone
• 由来する生物種: Bombyx mori (domestic silkworm)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 67729.45

構造登録者

Guo, P.C.,Zhang, Y.S.,Zhang, l.,Xu, H.Y. (登録日: 2021-09-09, 公開日: 2022-09-28, 最終更新日: 2024-11-13)

主引用文献

Zhang, L.,Xu, H.,Zhang, Y.,Zhang, H.,Wang, Z.,Guo, P.,Zhao, P.
Structural characterization and functional analysis of juvenile hormone acid methyltransferase JHAMT3 from the silkworm, Bombyx mori.
Insect Biochem.Mol.Biol., 151:103863-103863, 2022

PubMed Abstract: Juvenile hormone acid methyltransferase (JHAMT) is a rate-limiting enzyme of juvenile hormone (JH) biosynthesis in insects. It transfers the methyl group of S-adenosyl methionine to either the carboxyl group of JH acids or farnesoic acid to produce JH. Six JHAMT paralogues have been identified in the silkworm (Bombyx mori); among them, JHAMT1 and JHAMT2 display a methyltransferase activity. Here, the three-dimensional crystal structure of inactive JHAMT3 and the binary complex of JHAMT3 with its cofactor S-adenosyl-l-homocysteine were determined through X-ray crystallization. Comparative structural analysis revealed that JHAMT3 adopted a similar structural pattern to that of functional JHAMT2, which comprised one core Rossmann fold domain and one substrate-binding domain. Similar to JHAMT2, JHAMT3 underwent a conformational change at the Rossmann fold domain because of cofactor binding, which promoted ligand accommodation. However, it exhibited a relatively rigid substrate-binding pocket compared with that of JHAMT2. JHAMT3 was also highly expressed in the silk gland of fourth- and fifth-instar B. mori larvae. The results of expression profiling combined with activity analysis suggested that JHAMT3 might function as a binding protein of JH acids for the regulation of JH acid titers. These findings provide a structural basis for enhancing the understanding of the physiological function of JHAMT3 and a rational framework for the development of potent and specific inhibitors of JHAMT family members.

PubMed: 36341863
DOI: 10.1016/j.ibmb.2022.103863

実験手法

X-RAY DIFFRACTION (2.53 Å)