1tqy

The Actinorhodin Ketosynthase/Chain Length Factor

spinqualitylabelsall models 1tqy, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1tqy is a 8 chain structure with sequence from Streptomyces coelicolor A3(2). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: ACE, MG, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ACTI1_STRCO Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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