1RWL

Extracellular domain of Mycobacterium tuberculosis PknD

Summary for 1RWL

• Entry DOI: 10.2210/pdb1rwl/pdb
• Related: 1RWI
• Descriptor: Serine/threonine-protein kinase pknD, CADMIUM ION (3 entities in total)
• Functional Keywords: beta propeller, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc, transferase
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 1
• Total formula weight: 28969.10

Authors

Good, M.C.,Greenstein, A.E.,Young, T.A.,Ng, H.L.,Alber, T.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2003-12-16, release date: 2004-04-27, Last modification date: 2023-08-23)

Primary citation

Good, M.C.,Greenstein, A.E.,Young, T.A.,Ng, H.L.,Alber, T.
Sensor Domain of the Mycobacterium tuberculosis Receptor Ser/Thr Protein Kinase, PknD, forms a Highly Symmetric beta Propeller.
J.Mol.Biol., 339:459-469, 2004

PubMed 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.

PubMed: 15136047
DOI: 10.1016/j.jmb.2004.03.063

Experimental method

X-RAY DIFFRACTION (1.9 Å)