1tqy

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1tqy, resolution 2.00Å

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The Actinorhodin Ketosynthase/Chain Length Factor

Overview

The synthesis of aromatic polyketides, such as actinorhodin, tetracycline, and doxorubicin, begins with the formation of a polyketide chain. In type, II polyketide synthases (PKSs), chains are polymerized by the, heterodimeric ketosynthase-chain length factor (KS-CLF). Here we present, the 2.0-A structure of the actinorhodin KS-CLF, which shows polyketides, being elongated inside an amphipathic tunnel approximately 17 A in length, at the heterodimer interface. The structure resolves many of the questions, about the roles of KS and CLF. Although CLF regulates chain length, it, does not have an active site; KS must catalyze both chain initiation and, elongation. We provide evidence that the first cyclization of the, polyketide occurs within the KS-CLF tunnel. The mechanistic details of, this central PKS polymerase could guide biosynthetic chemists in designing, new pharmaceuticals and polymers.

About this Structure

1TQY is a Protein complex structure of sequences from Bacteria and Streptomyces coelicolor with NA, MG and ACE as ligands. Active as Beta-ketoacyl-acyl-carrier-protein synthase I, with EC number 2.3.1.41 Full crystallographic information is available from OCA.

Reference

An antibiotic factory caught in action., Keatinge-Clay AT, Maltby DA, Medzihradszky KF, Khosla C, Stroud RM, Nat Struct Mol Biol. 2004 Sep;11(9):888-93. Epub 2004 Aug 1. PMID:15286722

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