| PeerJ | |
| Crystallization and structure analysis of the core motif of the Pks13 acyltransferase domain from Mycobacterium tuberculosis | |
| article | |
| Mingjing Yu1  Chao Dou1  Yijun Gu2  Wei Cheng1  | |
| [1] Department of Respiratory and Critical Care Medicine, West China Hospital, Sichuan University;National Center for Protein Science | |
| 关键词: Mycobacterium tuberculosis; Polyketide synthase 13; Acyltransferase; Protein structure; | |
| DOI : 10.7717/peerj.4728 | |
| 学科分类:社会科学、人文和艺术(综合) | |
| 来源: Inra | |
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【 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】
CC BY
【 预 览 】
| Files | Size | Format | View |
|---|---|---|---|
| RO202307100012611ZK.pdf | 8526KB |
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