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

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 Tubercul...

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Detalles Bibliográficos
Autores principales: Yu, Mingjing, Dou, Chao, Gu, Yijun, Cheng, Wei
Formato: Online Artículo Texto
Lenguaje:English
Publicado: PeerJ Inc. 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5944431/
https://www.ncbi.nlm.nih.gov/pubmed/29761048
http://dx.doi.org/10.7717/peerj.4728
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author Yu, Mingjing
Dou, Chao
Gu, Yijun
Cheng, Wei
author_facet Yu, Mingjing
Dou, Chao
Gu, Yijun
Cheng, Wei
author_sort Yu, Mingjing
collection PubMed
description 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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spelling pubmed-59444312018-05-14 Crystallization and structure analysis of the core motif of the Pks13 acyltransferase domain from Mycobacterium tuberculosis Yu, Mingjing Dou, Chao Gu, Yijun Cheng, Wei PeerJ Biochemistry 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. PeerJ Inc. 2018-05-07 /pmc/articles/PMC5944431/ /pubmed/29761048 http://dx.doi.org/10.7717/peerj.4728 Text en © 2018 Yu et al. http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ) and either DOI or URL of the article must be cited.
spellingShingle Biochemistry
Yu, Mingjing
Dou, Chao
Gu, Yijun
Cheng, Wei
Crystallization and structure analysis of the core motif of the Pks13 acyltransferase domain from Mycobacterium tuberculosis
title Crystallization and structure analysis of the core motif of the Pks13 acyltransferase domain from Mycobacterium tuberculosis
title_full Crystallization and structure analysis of the core motif of the Pks13 acyltransferase domain from Mycobacterium tuberculosis
title_fullStr Crystallization and structure analysis of the core motif of the Pks13 acyltransferase domain from Mycobacterium tuberculosis
title_full_unstemmed Crystallization and structure analysis of the core motif of the Pks13 acyltransferase domain from Mycobacterium tuberculosis
title_short Crystallization and structure analysis of the core motif of the Pks13 acyltransferase domain from Mycobacterium tuberculosis
title_sort crystallization and structure analysis of the core motif of the pks13 acyltransferase domain from mycobacterium tuberculosis
topic Biochemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5944431/
https://www.ncbi.nlm.nih.gov/pubmed/29761048
http://dx.doi.org/10.7717/peerj.4728
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AT douchao crystallizationandstructureanalysisofthecoremotifofthepks13acyltransferasedomainfrommycobacteriumtuberculosis
AT guyijun crystallizationandstructureanalysisofthecoremotifofthepks13acyltransferasedomainfrommycobacteriumtuberculosis
AT chengwei crystallizationandstructureanalysisofthecoremotifofthepks13acyltransferasedomainfrommycobacteriumtuberculosis