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- W2058034454 abstract "Diverse 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." @default.
- W2058034454 created "2016-06-24" @default.
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- W2058034454 creator A5086812348 @default.
- W2058034454 creator A5088939845 @default.
- W2058034454 date "2004-05-01" @default.
- W2058034454 modified "2023-10-16" @default.
- W2058034454 title "Sensor Domain of the Mycobacterium tuberculosis Receptor Ser/Thr Protein Kinase, PknD, forms a Highly Symmetric β Propeller" @default.
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- W2058034454 doi "https://doi.org/10.1016/j.jmb.2004.03.063" @default.
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