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

Mingjing Yu | Zendy; Chao Dou | Zendy; Yijun Gu | Zendy; Wei Cheng | Zendy

Open Access

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

Author(s) -

Mingjing Yu,

Chao Dou,

Yijun Gu,

Wei Cheng

Publication year - 2018

Publication title -

peerj

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.927

H-Index - 70

ISSN - 2167-8359

DOI - 10.7717/peerj.4728

Subject(s) - crystallization , mycobacterium tuberculosis , computational biology , tuberculosis , motif (music) , microbiology and biotechnology , biology , medicine , chemistry , pathology , physics , organic chemistry , acoustics

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.

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