Yu_2018_PeerJ_6_e4728

Reference

Title : Crystallization and structure analysis of the core motif of the Pks13 acyltransferase domain from Mycobacterium tuberculosis - Yu_2018_PeerJ_6_e4728
Author(s) : Yu M , Dou C , Gu Y , Cheng W
Ref : PeerJ , 6 :e4728 , 2018
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 A 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.

PubMedSearch : Yu_2018_PeerJ_6_e4728
PubMedID: 29761048
Gene_locus related to this paper: myctu-PKS13

Related information

Gene_locus myctu-PKS13

Citations formats

Yu M, Dou C, Gu Y, Cheng W (2018)
Crystallization and structure analysis of the core motif of the Pks13 acyltransferase domain from Mycobacterium tuberculosis
PeerJ 6 :e4728

Yu M, Dou C, Gu Y, Cheng W (2018)
PeerJ 6 :e4728