| Autor: |
Mingjing Yu, Chao Dou, Yijun Gu, Wei Cheng |
| Jazyk: |
angličtina |
| Rok vydání: |
2018 |
| Předmět: |
|
| Zdroj: |
PeerJ, Vol 6, p e4728 (2018) |
| Druh dokumentu: |
article |
| ISSN: |
2167-8359 |
| DOI: |
10.7717/peerj.4728 |
| Popis: |
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. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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