Czarnota, S., Baxter, N.J., Cliff, M.J. et al. (3 more authors) (2017) 1H, 15N, 13C backbone resonance assignments of human soluble catechol O-methyltransferase in complex with S-adenosyl-l-methionine and 3,5-dinitrocatechol. Biomolecular NMR Assignments, 11 (1). pp. 57-61. ISSN 1874-2718
Abstract
Catechol O-methyltransferase (COMT) is an enzyme that plays a major role in catechol neurotransmitter deactivation. Inhibition of COMT can increase neurotransmitter levels, which provides a means of treatment for Parkinson's disease, schizophrenia and depression. COMT exists as two isozymes: a soluble cytoplasmic form (S-COMT), expressed in the liver and kidneys and a membrane-bound form (MB-COMT), found mostly in the brain. Here we report the backbone (1)H, (15)N and (13)C chemical shift assignments of S-COMT in complex with S-adenosyl-L-methionine, 3,5-dinitrocatechol and Mg(2+). Assignments were obtained by heteronuclear multidimensional NMR spectroscopy. In total, 97 % of all backbone resonances were assigned in the complex, with 205 out of a possible 215 residues assigned in the (1)H-(15)N TROSY spectrum. Prediction of solution secondary structure from a chemical shift analysis using the TALOS+ webserver is in good agreement with published X-ray crystal structures.
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Copyright, Publisher and Additional Information: | © The Author(s) 2016. This article is published with open access at Springerlink.com. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http:// creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. | ||||
Keywords: | Backbone resonance assignment; Enzyme; S-adenosyl-L-methionine; Transverse relaxation optimized spectroscopy; Triple-labelled Protein | ||||
Dates: |
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Institution: | The University of Sheffield | ||||
Academic Units: | The University of Sheffield > Faculty of Science (Sheffield) > School of Biosciences (Sheffield) > Department of Molecular Biology and Biotechnology (Sheffield) | ||||
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Depositing User: | Symplectic Sheffield | ||||
Date Deposited: | 05 Jan 2017 16:45 | ||||
Last Modified: | 30 Jun 2023 15:29 | ||||
Published Version: | https://doi.org/10.1007/s12104-016-9720-9 | ||||
Status: | Published | ||||
Publisher: | Springer Verlag | ||||
Refereed: | Yes | ||||
Identification Number: | https://doi.org/10.1007/s12104-016-9720-9 | ||||
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