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

PeerJ

Wei Cheng¹  Chao Dou¹  Mingjing Yu¹  Yijun Gu² 

[1] Department of Respiratory and Critical Care Medicine, West China Hospital, Sichuan University, Chengdu, Sichuan, People’s Republic of China;National Center for Protein Science, Shanghai, People’s Republic of China;

关键词: Mycobacterium tuberculosis;    Polyketide synthase 13;    Acyltransferase;    Protein structure;   

DOI  :  10.7717/peerj.4728

来源: DOAJ

【 摘 要 】

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.

【 授权许可】

Unknown