Open AccessAn ATPase with a twist: A unique mechanism underlies the activity of the bacterial tyrosine kinase, Wzc
Author(s) -
Fatlum Hajredini,
Ranajeet Ghose
Publication year - 2021
Publication title -
science advances
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.928
H-Index - 146
ISSN - 2375-2548
DOI - 10.1126/sciadv.abj5836
Subject(s) - arginine kinase , biochemistry , kinase , phosphorylation , biology , tyrosine , adenosine triphosphate , protein kinase domain , microbiology and biotechnology , sh3 domain , chemistry , arginine , proto oncogene tyrosine protein kinase src , amino acid , gene , mutant
While BY-kinases share many common features with P-loop enzymes, these are uniquely deployed for tyrosine phosphorylation.
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