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Structural insights into biosynthesis of resorcinolic lipids by a type III polyketide synthase in Neurospora crassa.

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.

journal_name

J Struct Biol

journal_title

Journal of structural biology

authors

Goyal A,Saxena P,Rahman A,Singh PK,Kasbekar DP,Gokhale RS,Sankaranarayanan R

doi

10.1016/j.jsb.2008.02.009

subject

Has Abstract

pub_date

2008-06-01 00:00:00

pages

411-21

issue

3

eissn

1047-8477

issn

1095-8657

pii

S1047-8477(08)00034-8

journal_volume

162

pub_type

杂志文章

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