Long-range dynamic correlations regulate the catalytic activity of the bacterial tyrosine kinase Wzc

descriptionPublicationkeyboard_double_arrow_right Article 18 Dec 2020 English Publisher:American Association for the Advancement of Science (AAAS)Journal:Science Advances, volume 6 (eissn: 2375-2548,

Copyright policy )Funded by:NSF | EAGER: Nature of the Pre-..., NSF | Activation and Regulation...

Authors: Fatlum Hajredini; Andrea Piserchio; Ranajeet Ghose;

doi: 10.1126/sciadv.abd3718

pmid: 33355134

pmc: PMC11206214

Long-range dynamic correlations regulate the catalytic activity of the bacterial tyrosine kinase Wzc

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Abstract

A mechanism for nucleotide exchange and activation is proposed for a family of protein tyrosine kinases unique to bacteria.

Related Organizations

CUNY City College
United States
City University of New York
United States
City College of New York
United States
The Graduate Center, CUNY
United States

Keywords

Adenosine Diphosphate, Adenosine Triphosphate, Escherichia coli Proteins, Escherichia coli, Membrane Proteins, Protein-Tyrosine Kinases, Research Articles

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