4q20 | pdb_00004q20

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

spinqualitylabelsall models 4q20, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4q20 is a 2 chain structure with sequence from Caucr. This structure supersedes the now removed PDB entry 4ew8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: divL, CC_3484 (CAUCR) Activity: Histidine kinase, with EC number 2.7.13.3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [DIVL_CAUCR] Required for cell division and growth. It catalyzes the phosphorylation of CtrA and activates transcription in vitro of the cell cycle-regulated fliF promoter. Publication Abstract from PubMed 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 approximately 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. Cell fate regulation governed by a repurposed bacterial histidine kinase.,Childers WS, Xu Q, Mann TH, Mathews II, Blair JA, Deacon AM, Shapiro L PLoS Biol. 2014 Oct 28;12(10):e1001979. doi: 10.1371/journal.pbio.1001979., eCollection 2014 Oct. PMID:25349992 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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