1p0z | pdb_00001p0z

Sensor Kinase CitA binding domain

spinqualitylabelsall models 1p0z, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1p0z is a 10 chain structure with sequence from "bacillus_pneumoniae"_(schroeter_1886)_flugge_1886 "bacillus pneumoniae" (schroeter 1886) flugge 1886. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FLC, MO7, NA, OMO Gene: CITA ("Bacillus pneumoniae" (Schroeter 1886) Flugge 1886) Activity: Histidine kinase, with EC number 2.7.13.3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CITA_KLEPN] Member of the two-component regulatory system CitA/CitB. Probably activates CitB by phosphorylation. The periplasmic domain binds H-citrate(2-), which is essential for induction of the citrate-fermentation genes. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The integral membrane sensor kinase CitA of Klebsiella pneumoniae is part of a two-component signal transduction system that regulates the transport and metabolism of citrate in response to its environmental concentration. Two-component systems are widely used by bacteria for such adaptive processes, but the stereochemistry of periplasmic ligand binding and the mechanism of signal transduction across the membrane remain poorly understood. The crystal structure of the CitAP periplasmic sensor domain in complex with citrate reveals a PAS fold, a versatile ligand-binding structural motif that has not previously been observed outside the cytoplasm or implicated in the transduction of conformational signals across the membrane. Citrate is bound in a pocket that is shared among many PAS domains but that shows structural variation according to the nature of the bound ligand. In CitAP, some of the citrate contact residues are located in the final strand of the central beta-sheet, which is connected to the C-terminal transmembrane helix. These secondary structure elements thus provide a potential conformational link between the periplasmic ligand binding site and the cytoplasmic signaling domains of the receptor. The structure of the periplasmic ligand-binding domain of the sensor kinase CitA reveals the first extracellular PAS domain.,Reinelt S, Hofmann E, Gerharz T, Bott M, Madden DR J Biol Chem. 2003 Oct 3;278(40):39189-96. Epub 2003 Jul 16. PMID:12867417 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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