1q9j

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(New page: 200px<br /><applet load="1q9j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q9j, resolution 2.75&Aring;" /> '''Structure of polyket...)
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Revision as of 22:23, 20 November 2007


1q9j, resolution 2.75Å

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Structure of polyketide synthase associated protein 5 from Mycobacterium tuberculosis

Overview

Polyketide-associated protein A5 (PapA5) is an acyltransferase that is, involved in production of phthiocerol and phthiodiolone dimycocerosate, esters, a class of virulence-enhancing lipids produced by Mycobacterium, tuberculosis. Structural analysis of PapA5 at 2.75-A resolution reveals a, two-domain structure that shares unexpected similarity to structures of, chloramphenicol acetyltransferase, dihydrolipoyl transacetylase, carnitine, acetyltransferase, and VibH, a non-ribosomal peptide synthesis, condensation enzyme. The PapA5 active site includes conserved histidine, and aspartic acid residues that are critical to PapA5 acyltransferase, activity. PapA5 catalyzes acyl transfer reactions on model substrates that, contain long aliphatic carbon chains, and two hydrophobic channels were, observed linking the PapA5 surface to the active site with properties, consistent with these biochemical activities and substrate preferences. An, additional alpha helix not observed in other acyltransferase structures, blocks the putative entrance into the PapA5 active site, indicating that, conformational changes may be associated with PapA5 activity. PapA5, represents the first structure solved for a protein involved in polyketide, synthesis in Mycobacteria.

About this Structure

1Q9J is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

Crystal structure of PapA5, a phthiocerol dimycocerosyl transferase from Mycobacterium tuberculosis., Buglino J, Onwueme KC, Ferreras JA, Quadri LE, Lima CD, J Biol Chem. 2004 Jul 16;279(29):30634-42. Epub 2004 May 3. PMID:15123643

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