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

Luping Pang; Vladimir Zanki; Sergei V. Strelkov; Arthur Van Aerschot; Ita Gruic-Sovulj; Stephen D. Weeks

doi:10.1038/s42003-022-03825-8

Communications Biology (Aug 2022)

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

Luping Pang,
Vladimir Zanki,
Sergei V. Strelkov,
Arthur Van Aerschot,
Ita Gruic-Sovulj,
Stephen D. Weeks

Affiliations

Luping Pang: Biocrystallography, Department of Pharmaceutical and Pharmacological Sciences, KU Leuven
Vladimir Zanki: Department of Chemistry, Faculty of Science, University of Zagreb
Sergei V. Strelkov: Biocrystallography, Department of Pharmaceutical and Pharmacological Sciences, KU Leuven
Arthur Van Aerschot: Medicinal Chemistry, Rega Institute for Medical Research, Department of Pharmaceutical and Pharmacological Sciences, KU Leuven
Ita Gruic-Sovulj: Department of Chemistry, Faculty of Science, University of Zagreb
Stephen D. Weeks: Biocrystallography, Department of Pharmaceutical and Pharmacological Sciences, KU Leuven

DOI: https://doi.org/10.1038/s42003-022-03825-8
Journal volume & issue: Vol. 5, no. 1
pp. 1 – 12

Abstract

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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.

Published in Communications Biology

ISSN: 2399-3642 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science: Biology (General)
Website: https://www.nature.com/commsbio/

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