3E1H

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

Summary for 3E1H

• Entry DOI: 10.2210/pdb3e1h/pdb
• Descriptor: Putative uncharacterized protein (2 entities in total)
• Functional Keywords: resorcinolic lipid synthase, type iii pks, acyltransferase, transferase
• Biological source: Neurospora crassa
• Total number of polymer chains: 2
• Total formula weight: 99185.77

Authors

Goyal, A.,Rahman, A.,Sankaranarayanan, R. (deposition date: 2008-08-04, release date: 2008-08-26, Last modification date: 2023-11-01)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.58 Å)