4esq | pdb_00004esq

Crystal structure of the extracellular domain of PknH from Mycobacterium tuberculosis

spinqualitylabelsall models 4esq, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4esq is a 1 chain structure with sequence from Mycobacterium tuberculosis h37rv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BTB, TB Gene: pknH, Rv1266c (Mycobacterium tuberculosis H37Rv) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Since their discovery over 20years ago, eukaryotic-like transmembrane receptor Ser/Thr protein kinases (STPKs) have been shown to play critical roles in the virulence, growth, persistence, and reactivation of many bacteria. Information regarding the signals transmitted by these proteins, however, remains scarce. To enhance understanding of the basis for STPK receptor signaling, we determined the 1.7-A-resolution crystal structure of the extracellular sensor domain of the Mycobacterium tuberculosis receptor STPK, PknH (Rv1266c). The PknH sensor domain adopts an unanticipated fold containing two intramolecular disulfide bonds and a large hydrophobic and polar cleft. The residues lining the cleft and those surrounding the disulfide bonds are conserved. These results suggest that PknH binds a small-molecule ligand that signals by changing the location or quaternary structure of the kinase domain. Structure of the Sensor Domain of Mycobacterium tuberculosis PknH Receptor Kinase Reveals a Conserved Binding Cleft.,Cavazos A, Prigozhin DM, Alber T J Mol Biol. 2012 Jun 20. PMID:22727744 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Serine/threonine protein kinase

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