Partitioning of the initial catalytic steps of leucyl-tRNA synthetase is driven by an active site peptide-plane flip

Crystal structures for all enzyme states of leucyl-tRNA synthetase in Neisseria gonorrhoeae reveal multi-domain conformational changes that correlate with a local peptide-plane flip in the active site to compartmentalize catalytic steps.

Bibliographic Details
Main Authors: Luping Pang, Vladimir Zanki, Sergei V. Strelkov, Arthur Van Aerschot, Ita Gruic-Sovulj, Stephen D. Weeks
Format: Article
Language:English
Published: Nature Portfolio 2022-08-01
Series:Communications Biology
Online Access:https://doi.org/10.1038/s42003-022-03825-8
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author Luping Pang
Vladimir Zanki
Sergei V. Strelkov
Arthur Van Aerschot
Ita Gruic-Sovulj
Stephen D. Weeks
author_facet Luping Pang
Vladimir Zanki
Sergei V. Strelkov
Arthur Van Aerschot
Ita Gruic-Sovulj
Stephen D. Weeks
author_sort Luping Pang
collection DOAJ
description Crystal structures for all enzyme states of leucyl-tRNA synthetase in Neisseria gonorrhoeae reveal multi-domain conformational changes that correlate with a local peptide-plane flip in the active site to compartmentalize catalytic steps.
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spelling doaj.art-281daae9c0c5428fb6d7c6d3b73993ac2022-12-22T04:05:16ZengNature PortfolioCommunications Biology2399-36422022-08-015111210.1038/s42003-022-03825-8Partitioning of the initial catalytic steps of leucyl-tRNA synthetase is driven by an active site peptide-plane flipLuping Pang0Vladimir Zanki1Sergei V. Strelkov2Arthur Van Aerschot3Ita Gruic-Sovulj4Stephen D. Weeks5Biocrystallography, Department of Pharmaceutical and Pharmacological Sciences, KU LeuvenDepartment of Chemistry, Faculty of Science, University of ZagrebBiocrystallography, Department of Pharmaceutical and Pharmacological Sciences, KU LeuvenMedicinal Chemistry, Rega Institute for Medical Research, Department of Pharmaceutical and Pharmacological Sciences, KU LeuvenDepartment of Chemistry, Faculty of Science, University of ZagrebBiocrystallography, Department of Pharmaceutical and Pharmacological Sciences, KU LeuvenCrystal structures for all enzyme states of leucyl-tRNA synthetase in Neisseria gonorrhoeae reveal multi-domain conformational changes that correlate with a local peptide-plane flip in the active site to compartmentalize catalytic steps.https://doi.org/10.1038/s42003-022-03825-8
spellingShingle Luping Pang
Vladimir Zanki
Sergei V. Strelkov
Arthur Van Aerschot
Ita Gruic-Sovulj
Stephen D. Weeks
Partitioning of the initial catalytic steps of leucyl-tRNA synthetase is driven by an active site peptide-plane flip
Communications Biology
title Partitioning of the initial catalytic steps of leucyl-tRNA synthetase is driven by an active site peptide-plane flip
title_full Partitioning of the initial catalytic steps of leucyl-tRNA synthetase is driven by an active site peptide-plane flip
title_fullStr Partitioning of the initial catalytic steps of leucyl-tRNA synthetase is driven by an active site peptide-plane flip
title_full_unstemmed Partitioning of the initial catalytic steps of leucyl-tRNA synthetase is driven by an active site peptide-plane flip
title_short Partitioning of the initial catalytic steps of leucyl-tRNA synthetase is driven by an active site peptide-plane flip
title_sort partitioning of the initial catalytic steps of leucyl trna synthetase is driven by an active site peptide plane flip
url https://doi.org/10.1038/s42003-022-03825-8
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