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Partitioning of the initial catalytic steps of leucyl-tRNA synthetase is driven by an active site peptide-plane flip
- Source :
- Communications Biology, Vol 5, Iss 1, Pp 1-12 (2022)
- Publication Year :
- 2022
- Publisher :
- Nature Portfolio, 2022.
-
Abstract
- 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.
- Subjects :
- Biology (General)
QH301-705.5
Subjects
Details
- Language :
- English
- ISSN :
- 23993642
- Volume :
- 5
- Issue :
- 1
- Database :
- Directory of Open Access Journals
- Journal :
- Communications Biology
- Publication Type :
- Academic Journal
- Accession number :
- edsdoj.281daae9c0c5428fb6d7c6d3b73993ac
- Document Type :
- article
- Full Text :
- https://doi.org/10.1038/s42003-022-03825-8