3E1H

Crystal structure of a type III polyketide synthase PKSIIINc from Neurospora crassa

3E1H の概要

• エントリーDOI: 10.2210/pdb3e1h/pdb
• 分子名称: Putative uncharacterized protein (2 entities in total)
• 機能のキーワード: resorcinolic lipid synthase, type iii pks, acyltransferase, transferase
• 由来する生物種: Neurospora crassa
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 99185.77

構造登録者

Goyal, A.,Rahman, A.,Sankaranarayanan, R. (登録日: 2008-08-04, 公開日: 2008-08-26, 最終更新日: 2023-11-01)

主引用文献

Goyal, A.,Saxena, P.,Rahman, A.,Singh, P.K.,Kasbekar, D.P.,Gokhale, R.S.,Sankaranarayanan, R.
Structural insights into biosynthesis of resorcinolic lipids by a type III polyketide synthase in Neurospora crassa
J.Struct.Biol., 162:411-421, 2008

PubMed Abstract: Microbial type III polyketide synthases (PKSs) have revealed remarkable mechanistic as well as functional versatility. Recently, a type III PKS homolog from Azotobacter has been implicated in the biosynthesis of resorcinolic lipids, thus adding a new functional significance to this class of proteins. Here, we report the structural and mutational investigations of a novel type III PKS protein from Neurospora crassa involved in the biosynthesis of resorcinolic metabolites by utilizing long chain fatty acyl-CoAs. The structure revealed a long hydrophobic tunnel responsible for its fatty acyl chain length specificity resembling that of PKS18, a mycobacterial type III PKS. Structure-based mutational studies to block the tunnel not only altered the fatty acyl chain specificity but also resulted in change of cyclization pattern affecting the product profile. This first structural characterization of a resorcinolic lipid synthase provides insights into the coordinated functioning of cyclization and a substrate-binding pocket, which shows mechanistic intricacy underlying type III PKS catalysis.

PubMed: 18462950
DOI: 10.1016/j.jsb.2008.02.009

実験手法

X-RAY DIFFRACTION (2.58 Å)