Chemical shift assignment of residues 1-147 of M. tuberculosis protein kinase G (PknG) including the natively disordered N-terminus and the reduced, metal bound rubredoxin-like domain

Protein kinase G (PknG) 1-147 natively disordered region + rubredoxin domain reduced, metal bound form

The eukaryotic like serine /threonine protein kinase G promotes cellular survival of pathogenic mycobacteria by inhibiting phagosome-lysosome fusion within host macophages.

Crystal structure of PknG 73-750 in complex with the inhibitor AX20017

Crystal structure of PknG 64-405 in complex with ADP

Crystal structure of PknG 64-405 in complex with AGS

Chemical shift assignment of the intrinsically disordered N-terminus and the rubredoxin domain in the folded metal bound and unfolded oxidized state of mycobacterial protein kinase G.

His-PknG 1-147 contains the NORS region & rubredoxin motif of mycobacterial protein kinase G
21, M = the first aminoacid of the protein sequence
Residue 1-20 represents a non native poly histidine tag

Regulatory N-terminal regions of a ser/thr kinase

Chemical shift assignment of the natively disordered N-terminus (= NORS, residues 1-75) of M. tuberculosis protein kinase G (PknG)

Chemical shift assignment of the oxidized, unfolded rubredoxin-like domain (= RD, residues 74-147) of M. tuberculosis protein kinase G (PknG)

Chemical shift assignment of the reduced, metal bound rubredoxin-like domain (= RD, residues 74-147) of M. tuberculosis protein kinase G (PknG)

PknG 1-147 / rubredoxin domain in metal bound state (reduced) / with coordinated Zn - ion

Technical University of Munich, Department of Chemistry, Biomolecular NMR

Institute of Structural Biology, Helmholtz Zentrum Munich

Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax