Mechanistic Insights Revealed by the Crystal Structure of a Histidine Kinase with Signal Transducer and Sensor Domains
Author(s) -
Chen Wang,
Jiayan Sang,
Jiawei Wang,
Ming-yan Su,
Jennifer S. Downey,
Qinggan Wu,
Shida Wang,
Yongfei Cai,
Xiaozheng Xu,
Jun Wu,
Dilani B. Senadheera,
Dennis G. Cvitkovitch,
Lin Chen,
Steven D. Goodman,
Aidong Han
Publication year - 2013
Publication title -
plos biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.127
H-Index - 271
eISSN - 1545-7885
pISSN - 1544-9173
DOI - 10.1371/journal.pbio.1001493
Subject(s) - histidine kinase , response regulator , biology , biophysics , phosphatase , hamp domain , phosphorylation , histidine , dimer , kinase , biochemistry , crystallography , microbiology and biotechnology , binding site , nuclear magnetic resonance , chemistry , physics , amino acid , binding domain , gene , mutant
A crystal structure reveals an elegant mechanistic switch whereby helical bending and catalytic domain rotation allow self-activation of a histidine kinase during a bacterial stress response.
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