Crystallization and structure analysis of the core motif of the Pks13 acyltransferase domain from Mycobacterium tuberculosis

Mingjing Yu; Chao Dou; Yijun Gu; Wei Cheng

doi:10.7717/peerj.4728

Crystallization and structure analysis of the core motif of the Pks13 acyltransferase domain from Mycobacterium tuberculosis

PeerJ. 2018 May 7:6:e4728. doi: 10.7717/peerj.4728. eCollection 2018.

Authors

Mingjing Yu^#¹, Chao Dou^#¹, Yijun Gu², Wei Cheng¹

Affiliations

¹ Department of Respiratory and Critical Care Medicine, West China Hospital, Sichuan University, Chengdu, Sichuan, People's Republic of China.
² National Center for Protein Science, Shanghai, People's Republic of China.

^# Contributed equally.

Abstract

Type I polyketide synthase 13 (Pks13) is involved in the final step of the biosynthesis of mycolic acid in Mycobacterium tuberculosis. Recent articles have reported that Pks13 is an essential enzyme in the mycolic acid biosynthesis pathway, and it has been deeply studied as a drug target in Tuberculosis. We report a high-resolution structure of the acyltransferase (AT) domain of Pks13 at 2.59 Å resolution. Structural comparison with the full-length AT domain (PDB code, 3TZW, and 3TZZ) reveals a different orientation of the C-terminal helix and rearrangement of some conserved residues.

Keywords: Acyltransferase; Mycobacterium tuberculosis; Polyketide synthase 13; Protein structure.

Grants and funding

This work was supported by the National Natural Science Foundation of China (No. 00402354011009). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.