3a0w | pdb_00003a0w

Catalytic domain of histidine kinase ThkA (TM1359) for MAD phasing (nucleotide free form 2, orthorombic)

spinqualitylabelsall models 3a0w, resolution 1.69Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3a0w is a 2 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.69Å Ligands: EMC, EMT, MPD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9X180_THEMA 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 We determined the structure of the complex of the sensory histidine kinase (HK) and its cognate response regulator (RR) in the two-component signal transduction system of Thermotoga maritima. This was accomplished by fitting the high-resolution structures of the isolated HK domains and the RR onto the electron density map (3.8 A resolution) of the HK/RR complex crystal. Based on the structural information, we evaluated the roles of both interdomain and intermolecular interactions in the signal transduction of the cytosolic PAS-linked HK and RR system, in particular the O(2)-sensor FixL/FixJ system. The PAS-sensor domain of HK interacts with the catalytic domain of the same polypeptide chain by creating an interdomain beta sheet. The interaction site between HK and RR, which was confirmed by NMR, is suitable for the intermolecular transfer reaction of the phosphoryl group, indicating that the observed interaction is important for the phosphatase activity of HK that dephosphorylates phospho-RR. Structure of PAS-linked histidine kinase and the response regulator complex.,Yamada S, Sugimoto H, Kobayashi M, Ohno A, Nakamura H, Shiro Y Structure. 2009 Oct 14;17(10):1333-44. PMID:19836334 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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