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Crystallization and structure analysis of the core motif of the Pks13 acyltransferase domain from Mycobacterium tuberculosis.
Yu, Mingjing; Dou, Chao; Gu, Yijun; Cheng, Wei.
Afiliación
  • Yu M; Department of Respiratory and Critical Care Medicine, West China Hospital, Sichuan University, Chengdu, Sichuan, People's Republic of China.
  • Dou C; Department of Respiratory and Critical Care Medicine, West China Hospital, Sichuan University, Chengdu, Sichuan, People's Republic of China.
  • Gu Y; National Center for Protein Science, Shanghai, People's Republic of China.
  • Cheng W; Department of Respiratory and Critical Care Medicine, West China Hospital, Sichuan University, Chengdu, Sichuan, People's Republic of China.
PeerJ ; 6: e4728, 2018.
Article en En | MEDLINE | ID: mdl-29761048
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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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: PeerJ Año: 2018 Tipo del documento: Article Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: PeerJ Año: 2018 Tipo del documento: Article Pais de publicación: Estados Unidos