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  The crystal structure of mycobacterial epoxide hydrolase A

Schulz, E.-C., Henderson, S. R., Illarionov, B., Crosskey, T., Southall, S. M., Krichel, B., et al. (2020). The crystal structure of mycobacterial epoxide hydrolase A. Scientific Reports, 10(1): 16539. doi:10.1038/s41598-020-73452-y.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0007-36FC-1 Version Permalink: http://hdl.handle.net/21.11116/0000-0007-36FD-0
Genre: Journal Article

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Open Access. - This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder.
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41598_2020_73452_MOESM1_ESM.pdf (Supplementary material), 9MB
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https://dx.doi.org/10.1038/s41598-020-73452-y (Publisher version)
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Schulz, E.-C.1, 2, Author              
Henderson, S. R.2, Author
Illarionov, B.3, Author
Crosskey, T.2, Author
Southall, S. M.2, Author
Krichel, B.4, Author
Uetrecht, C.5, Author
Fischer, M.3, Author
Wilmanns, M.2, 6, Author
Affiliations:
1Miller Group, Atomically Resolved Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society, ou_1938288              
2European Molecular Biology Laboratory, Hamburg Unit, ou_persistent22              
3Hamburg School of Food Science, Institute of Food Chemistry, Universität Hamburg, ou_persistent22              
4Heinrich Pette Institute, Leibniz Institute for Experimental Virology, ou_persistent22              
5European XFEL GmbH, ou_persistent22              
6University of Hamburg Medical Center Hamburg-Eppendorf, ou_persistent22              

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 Abstract: The human pathogen Mycobacterium tuberculosis is the causative agent of tuberculosis resulting in over 1 million fatalities every year, despite decades of research into the development of new anti-TB compounds. Unlike most other organisms M. tuberculosis has six putative genes for epoxide hydrolases (EH) of the α/β-hydrolase family with little known about their individual substrates, suggesting functional significance for these genes to the organism. Due to their role in detoxification, M. tuberculosis EH’s have been identified as potential drug targets. Here, we demonstrate epoxide hydrolase activity of M. thermoresistibile epoxide hydrolase A (Mth-EphA) and report its crystal structure in complex with the inhibitor 1,3-diphenylurea at 2.0 Å resolution. Mth-EphA displays high sequence similarity to its orthologue from M. tuberculosis and generally high structural similarity to α/β-hydrolase EHs. The structure of the inhibitor bound complex reveals the geometry of the catalytic residues and the conformation of the inhibitor. Comparison to other EHs from mycobacteria allows insight into the active site plasticity with respect to substrate specificity. We speculate that mycobacterial EHs may have a narrow substrate specificity providing a potential explanation for the genetic repertoire of epoxide hydrolase genes in M. tuberculosis.

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Language(s): eng - English
 Dates: 2019-09-302020-09-162020-10-06
 Publication Status: Published online
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 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s41598-020-73452-y
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Title: Scientific Reports
  Abbreviation : Sci. Rep.
Source Genre: Journal
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Publ. Info: London, UK : Nature Publishing Group
Pages: - Volume / Issue: 10 (1) Sequence Number: 16539 Start / End Page: - Identifier: ISSN: 2045-2322
CoNE: https://pure.mpg.de/cone/journals/resource/2045-2322