Biochemical and Structural Study of the Atypical Acyltransferase Domain from the Mycobacterial Polyketide Synthase Pks13

Fabien Bergeret (1) , Sabine Gavalda (1) , Christian Chalut (1) , Wladimir Malaga (1) , Annaïk Quémard (1) , Jean-Denis Pedelacq (1) , Mamadou Daffé (1) , Christophe Guilhot (1) , Lionel Mourey (1) , Cécile Bon (1)

1 IPBS - Institut de pharmacologie et de biologie structurale

Background: Pks13 is involved in the final biosynthesis step of mycolic acids. Results: We report the full characterization of a 52-kDa fragment containing the acyltransferase domain of Pks13. Conclusion: Pks13 is able to load unusually long chain acyl-CoAs through an unprecedented hydrophobic channel. Significance: This study could constitute a key step toward the development of new antibiotics against mycobacterial infections.

Domaines: Sciences du Vivant [q-bio]

Fabien Bergeret, Sabine Gavalda, Christian Chalut, Wladimir Malaga, Annaïk Quémard, et al.. Biochemical and Structural Study of the Atypical Acyltransferase Domain from the Mycobacterial Polyketide Synthase Pks13. Journal of Biological Chemistry, 2012, 287, pp.33675 - 33690. ⟨10.1074/jbc.m111.325639⟩. ⟨hal-03003064⟩