6K97

Crystal structure of fusion DH domain

6K97 の概要

• エントリーDOI: 10.2210/pdb6k97/pdb
• 分子名称: Fusion DH, SULFATE ION (3 entities in total)
• 機能のキーワード: double hot dog fold, polyketide synthase, dehydratase, cremimycin biosynthesis, lyase
• 由来する生物種: Streptomyces sp. MJ635-86F5; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 70764.75

構造登録者

Kawasaki, D.,Miyanaga, A.,Chisuga, T.,Kudo, F.,Eguchi, T. (登録日: 2019-06-14, 公開日: 2019-11-27, 最終更新日: 2023-11-22)

主引用文献

Kawasaki, D.,Miyanaga, A.,Chisuga, T.,Kudo, F.,Eguchi, T.
Functional and Structural Analyses of the Split-Dehydratase Domain in the Biosynthesis of Macrolactam Polyketide Cremimycin.
Biochemistry, 58:4799-4803, 2019

PubMed Abstract: In the biosynthesis of the macrolactam antibiotic cremimycin, the 3-aminononanoic acid starter unit is formed via a non-2-enoyl acyl carrier protein thioester intermediate, which is presumed to be constructed by -acyltransferase (AT) polyketide synthases (PKSs) CmiP2, CmiP3, and CmiP4. While canonical -AT PKS modules are comprised of a single polypeptide, the PKS module formed by CmiP2 and CmiP3 is split within the dehydratase (DH) domain. Here, we report the enzymatic function and the structural features of this split-DH domain. analysis showed that the split-DH domain catalyzes the dehydration reaction of ()-3-hydroxynonanoyl -acetylcysteamine thioester (SNAC) to form ()-non-2-enoyl-SNAC, suggesting that the split-DH domain is catalytically active in cremimycin biosynthesis. In addition, structural analysis revealed that the CmiP2 and CmiP3 subunits of the split-DH domain form a tightly associated heterodimer through several hydrogen bonding and hydrophobic interactions, which are similar to those of canonical DH domains of other -AT PKSs. These results indicate that the split-DH domain has the same function and structure as common -AT PKS DH domains.

PubMed: 31721563
DOI: 10.1021/acs.biochem.9b00897

実験手法

X-RAY DIFFRACTION (2.5 Å)