Open AccessHigh-resolution structures of a siderophore-producing cyclization domain from Yersinia pestis offer a refined proposal of substrate binding
Author(s) -
Andrew Gnann,
Yuan Xia,
Jess Soule,
Clara Barthélemy,
Jayata S. Mawani,
Sarah Nzikoba Musoke,
Brian M. Castellano,
Edward J. Brignole,
Dominique P. Frueh,
Daniel P. Dowling
Publication year - 2022
Publication title -
journal of biological chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.361
H-Index - 513
eISSN - 1067-8816
pISSN - 0021-9258
DOI - 10.1016/j.jbc.2022.102454
Subject(s) - nonribosomal peptide , yersinia pestis , siderophore , yersinia , chemistry , stereochemistry , virulence , binding site , thiazoline , active site , combinatorial chemistry , catalysis , biochemistry , biology , bacteria , enzyme , biosynthesis , genetics , gene
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