3TZZ

Crystal structure of a fragment containing the acyltransferase domain of Pks13 from Mycobacterium tuberculosis in the carboxypalmitoylated form at 2.5 A

3TZZ の概要

• エントリーDOI: 10.2210/pdb3tzz/pdb
• 関連するPDBエントリー: 3TZW 3TZX 3TZY
• 分子名称: Polyketide synthase PKS13, 12-mer peptide, tetradecylpropanedioic acid, ... (7 entities in total)
• 機能のキーワード: acyltransferase, long fatty acid chain transferase, acyl carrier protein, transferase
• 由来する生物種: Mycobacterium tuberculosis; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 109086.90

構造登録者

Bergeret, F.,Pedelacq, J.D.,Mourey, L.,Bon, C. (登録日: 2011-09-28, 公開日: 2012-08-29, 最終更新日: 2023-11-01)

主引用文献

Bergeret, F.,Gavalda, S.,Chalut, C.,Malaga, W.,Quemard, A.,Pedelacq, J.D.,Daffe, M.,Guilhot, C.,Mourey, L.,Bon, C.
Biochemical and structural study of the atypical acyltransferase domain from the mycobacterial polyketide synthase pks13
J.Biol.Chem., 287:33675-33690, 2012

PubMed Abstract: Pks13 is a type I polyketide synthase involved in the final biosynthesis step of mycolic acids, virulence factors, and essential components of the Mycobacterium tuberculosis envelope. Here, we report the biochemical and structural characterization of a 52-kDa fragment containing the acyltransferase domain of Pks13. This fragment retains the ability to load atypical extender units, unusually long chain acyl-CoA with a predilection for carboxylated substrates. High resolution crystal structures were determined for the apo, palmitoylated, and carboxypalmitoylated forms. Structural conservation with type I polyketide synthases and related fatty-acid synthases also extends to the interdomain connections. Subtle changes could be identified both in the active site and in the upstream and downstream linkers in line with the organization displayed by this singular polyketide synthase. More importantly, the crystallographic analysis illustrated for the first time how a long saturated chain can fit in the core structure of an acyltransferase domain through a dedicated channel. The structures also revealed the unexpected binding of a 12-mer peptide that might provide insight into domain-domain interaction.

PubMed: 22825853
DOI: 10.1074/jbc.M111.325639

実験手法

X-RAY DIFFRACTION (2.49 Å)