2KUD

NMR structure of the PASTA domain 1 and 2 of Mycobacterium tuberculosis of PknB

Summary for 2KUD

• Entry DOI: 10.2210/pdb2kud/pdb
• Related: 2KUE 2KUF 2KUI
• NMR Information: BMRB: 16732
• Descriptor: Serine/threonine-protein kinase pknB (1 entity in total)
• Functional Keywords: kinase, external domain, signaling, stpk, resuscitation, serine/threonine-protein kinase, transferase
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 1
• Total formula weight: 14530.21

Authors

Barthe, P.,Mukamolova, G.,Roumestand, C.,Cohen-Gonsaud, M. (deposition date: 2010-02-17, release date: 2010-04-14, Last modification date: 2024-05-15)

Primary citation

Barthe, P.,Mukamolova, G.V.,Roumestand, C.,Cohen-Gonsaud, M.
The structure of PknB extracellular PASTA domain from mycobacterium tuberculosis suggests a ligand-dependent kinase activation
Structure, 18:606-615, 2010

PubMed Abstract: PknB is a transmembrane Ser/Thr protein kinase that defines and belongs to an ultraconserved kinase subfamily found in Gram-positive bacteria. Essential for Mycobacterium tuberculosis growth, its close homolog in Bacillus subtilis has been linked to exit from dormancy. The kinase possesses an extracellular region composed of a repetition of PASTA domains, believed to bind peptidoglycan fragments that might act as a signaling molecule. We report here the first solution structure of this extracellular region. Small-angle X-ray scattering and nuclear magnetic resonance studies show that the four PASTA domains display an unexpected linear organization, contrary to what is observed in the distant protein PBP2x from Streptococccus pneumoniae where two PASTA domains fold over in a compact structure. We propose a model for PknB activation based on a ligand-dependent dimerization of the extracellular PASTA domains that initiates multiple signaling pathways.

PubMed: 20462494
DOI: 10.1016/j.str.2010.02.013

Experimental method

SOLUTION NMR