1rwl
From Proteopedia
Extracellular domain of Mycobacterium tuberculosis PknD
Structural highlights
FunctionPKND_MYCTU Key microbial factor required for central nervous system tuberculosis. Required for invasion of host brain endothelia, but not macrophages, lung epithelia or other endothelia. Phosphorylates the anti-anti-sigma factor homolog Rv0516c, which inhibits binding of Rv0516c to Rv2638, another anti-anti-sigma factor. Can also phosphorylate the FHA domain of Rv1747.[1] [2] [3] 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 PubMedDiverse pathogenic bacteria produce transmembrane receptor Ser/Thr protein kinases (STPKs), but little is known about the signals mediated by these "eukaryotic-like" proteins. To explore the basis for signaling in the bacterial STPK receptor family, we determined the structure of the sensor domain of Mycobacterium tuberculosis PknD. In two crystal forms, the PknD sensor domain forms a rigid, six-bladed beta-propeller with a flexible tether to the transmembrane domain. The PknD sensor domain is the most symmetric beta-propeller structure described. All residues that vary most among the blade subdomains cluster in the large "cup" motif, analogous to the ligand-binding surface in many beta-propeller proteins. These results suggest that PknD binds a multivalent ligand that signals by changing the quaternary structure of the intracellular kinase domain. Sensor domain of the Mycobacterium tuberculosis receptor Ser/Thr protein kinase, PknD, forms a highly symmetric beta propeller.,Good MC, Greenstein AE, Young TA, Ng HL, Alber T J Mol Biol. 2004 May 28;339(2):459-69. PMID:15136047[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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