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Wittwer, M.* ; Dames, S.A.

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.

Biomol. NMR Assign. 10, 401-406 (2016)
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Mycobacterium tuberculosis protein kinase G (PknG) is a 82 kDa multidomain eukaryotic-like serine/threonine kinase mediating the survival of pathogenic mycobacteria within host macrophages. The N-terminal sequence preceding the catalytic kinase domain contains an approximately 75 residues long tail, which was predicted to show no regulatory secondary structure (1–75 = NORS) but harbors the major in vivo phosphorylation site (T63), and a rubredoxin-like metal binding motif (74–147 = RD). In the reduced rubredoxin motif, four conserved cysteine residues that are present as two C-X-X-C-G motifs coordinate a metal ion. The cysteines are further involved in sensing the redox environment to regulate PknG catalytic activity. Here, we report the 1H, 13C, and 15N resonance assignments of the highly dynamic unstructured N-terminal region NORS and the RD in the reduced, metal bound, presumably folded and the oxidized, presumably unfolded state. Chemical shifts have been deposited at the BioMagResBank under the BMRB accession numbers 26,028 for the His-PknG1–147 with the RD in reduced, metal bound state, 26,027 for His-PknG1–75, and 26,030 and 26,029 for PknG74–147 either in the reduced, metal bound or oxidized state, respectively. The presented chemical shift assignments pave the route for the structural characterization of the regulation of PknG by redox changes and posttranslational modifications (phosphorylation).
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Chemical Shift Assignment ; Intrinsically Disordered Protein ; Mycobacterium Tuberculosis Protein Kinase G ; Nmr ; Redox-sensitive Metal Binding Motif ; Rubredoxin; Pathogenic Mycobacteria; Tuberculosis; Sensitivity; Macrophages; Resonances; Survival; Amide
ISSN (print) / ISBN 1874-2718
e-ISSN 1874-270X
Quellenangaben Band: 10, Heft: 2, Seiten: 401-406 Artikelnummer: , Supplement: ,
Verlag Springer
Verlagsort Dordrecht
Begutachtungsstatus Peer reviewed