5ukv | pdb_00005ukv

DHp domain of PhoR of M. tuberculosis - SeMet

spinqualitylabelsall models 5ukv, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ukv is a 2 chain structure with sequence from "bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EDO, K, PEG, PG0, PG4, PGE NonStd Res: MSE Related: 5uky Activity: Histidine kinase, with EC number 2.7.13.3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The PhoP-PhoR two-component system is essential for the virulence of Mycobacterium tuberculosis (Mtb) and therefore represents a potential target for developing novel antituberculosis therapies. However, little is known about the mechanism by which this two-component system regulates the virulence. In this study, we demonstrated that a phoR mutant Mtb strain has phenotypes similar to those of a phoP mutant, suggesting that PhoP and PhoR work in the same pathway to regulate Mtb virulence. We determined the structure of the dimerization and histidine phosphotransfer (DHp) domain of PhoR to a 1.9 A resolution. The structure revealed that the DHp domain is a dimer. Each subunit consists of two antiparallel alpha helices connected by a loop of five residues. The two subunits of the dimer fold into a four-helical bundle with a continuous hydrophobic core. The topology of the four-helical bundle is identical to the histidine kinases that are known to have a cis-autophosphorylation mechanism, suggesting that PhoR is likely to autophosphorylate in cis. The dimer is asymmetric, with one subunit having a greater bending angle than the other at the highly conserved proline residue five-residues downstream of the phosphorylation site histidine. This structural asymmetry of the dimer suggests the flexibility of the PhoR DHp domain, which is likely to be important for the signal transduction mechanism in controlling the autophosphorylation and phosphotransfer reactions and communicating with the upstream structure. Asymmetric Structure of the Dimerization Domain of PhoR, a Sensor Kinase Important for the Virulence of Mycobacterium tuberculosis.,Xing D, Ryndak MB, Wang L, Kolesnikova I, Smith I, Wang S ACS Omega. 2017 Jul 31;2(7):3509-3517. doi: 10.1021/acsomega.7b00612. Epub 2017, Jul 12. PMID:28782049 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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