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: 4EW8Summary for 4Q20
Entry DOI | 10.2210/pdb4q20/pdb |
Descriptor | Sensor protein DivL (2 entities in total) |
Functional Keywords | signal transduction, two-component regulatory system, hiska domain, ghkl domain, structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-biology, transferase |
Biological source | Caulobacter crescentus |
Cellular location | Cell membrane; Single-pass membrane protein: Q9RQQ9 |
Total number of polymer chains | 2 |
Total formula weight | 57728.98 |
Authors | Joint Center for Structural Genomics (JCSG) (deposition date: 2014-04-04, release date: 2014-04-23, Last modification date: 2024-02-28) |
Primary citation | Childers, 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: 25349992DOI: 10.1371/journal.pbio.1001979 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
Download full validation report