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4Q20

Crystal structure of a C-terminal part of tyrosine kinase (DivL) from Caulobacter crescentus CB15 at 2.50 A resolution (PSI Community Target, Shapiro)

Replaces:  4EW8
Summary for 4Q20
Entry DOI10.2210/pdb4q20/pdb
DescriptorSensor protein DivL (2 entities in total)
Functional Keywordssignal transduction, two-component regulatory system, hiska domain, ghkl domain, structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-biology, transferase
Biological sourceCaulobacter crescentus
Cellular locationCell membrane; Single-pass membrane protein: Q9RQQ9
Total number of polymer chains2
Total formula weight57728.98
Authors
Joint Center for Structural Genomics (JCSG) (deposition date: 2014-04-04, release date: 2014-04-23, Last modification date: 2024-02-28)
Primary citationChilders, W.S.,Xu, Q.,Mann, T.H.,Mathews, I.I.,Blair, J.A.,Deacon, A.M.,Shapiro, L.
Cell fate regulation governed by a repurposed bacterial histidine kinase.
Plos Biol., 12:e1001979-e1001979, 2014
Cited by
PubMed Abstract: One of the simplest organisms to divide asymmetrically is the bacterium Caulobacter crescentus. The DivL pseudo-histidine kinase, positioned at one cell pole, regulates cell-fate by controlling the activation of the global transcription factor CtrA via an interaction with the response regulator (RR) DivK. DivL uniquely contains a tyrosine at the histidine phosphorylation site, and can achieve these regulatory functions in vivo without kinase activity. Determination of the DivL crystal structure and biochemical analysis of wild-type and site-specific DivL mutants revealed that the DivL PAS domains regulate binding specificity for DivK∼P over DivK, which is modulated by an allosteric intramolecular interaction between adjacent domains. We discovered that DivL's catalytic domains have been repurposed as a phosphospecific RR input sensor, thereby reversing the flow of information observed in conventional histidine kinase (HK)-RR systems and coupling a complex network of signaling proteins for cell-fate regulation.
PubMed: 25349992
DOI: 10.1371/journal.pbio.1001979
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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