Ontology highlight
ABSTRACT:
SUBMITTER: Bachhawat P
PROVIDER: S-EPMC3685586 | biostudies-literature | 2005 Sep
REPOSITORIES: biostudies-literature
Bachhawat Priti P Swapna G V T GV Montelione Gaetano T GT Stock Ann M AM
Structure (London, England : 1993) 20050901 9
Response regulators (RRs), which undergo phosphorylation/dephosphorylation at aspartate residues, are highly prevalent in bacterial signal transduction. RRs typically contain an N-terminal receiver domain that regulates the activities of a C-terminal DNA binding domain in a phosphorylation-dependent manner. We present crystallography and solution NMR data for the receiver domain of Escherichia coli PhoB which show distinct 2-fold symmetric dimers in the inactive and active states. These structur ...[more]