7zp0

Crystal structure of CusS histidine kinase catalytic core from Escherichia coli

spinqualitylabelsall models 7zp0, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7zp0 is a 6 chain structure with sequence from Escherichia coli 'BL21-Gold(DE3)pLysS AG'. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.398Å Ligands: EDO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A2J1D710_ECOLX Member of a two-component regulatory system.[RuleBase:RU364088] Publication Abstract from PubMed The CusS histidine kinase is a member of Escherichia coli two-component signal transduction system, engaged in a response to copper ions excess in the cell periplasm. The periplasmic sensor domain of CusS binds the free copper ions and the CusS kinase core phosphorylates the cognate CusR which regulates transcription of the efflux pomp CusCBA. A small amount of copper ions is indispensable for the aerobic cell metabolism. Nonetheless, its excess in the cytoplasm generates damaging and reactive hydroxyl radicals. For that reason, understanding the bacterial copper sensing mechanisms can contribute to reducing bacterial copper-resistance and developing bactericidal copper-based materials. The crystal structure of the CusS kinase core was solved at the resolution of 1.4 A. The cytoplasmic catalytic core domains formed a homodimer. Based on the obtained structure, the intramolecular and intermolecular interactions crucial for the mechanism of CusS autophosphorylation were described. Crystal structure of the Escherichia coli CusS kinase core.,Cociurovscaia A, Bujacz G, Pietrzyk-Brzezinska AJ J Struct Biol. 2022 Jul 27;214(3):107883. doi: 10.1016/j.jsb.2022.107883. PMID:35907487 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA