TY  - JOUR
A1  - Niesteruk, Anna
A1  - Hutchison, Marie
A1  - Sreeramulu, Sridhar
A1  - Jonker, Hendrik R. A.
A1  - Richter, Christian
A1  - Abele, Rupert
A1  - Bock, Christoph
A1  - Schwalbe, Harald
T1  - Structural characterization of the intrinsically disordered domain of Mycobacterium tuberculosis protein tyrosine kinase A
N2  - Although intrinsically disordered proteins or protein domains (IDPs or IDD) are less abundant in bacteria than in eukaryotes, their presence in pathogenic bacterial proteins is important for protein-protein interactions. The protein tyrosine kinase A (PtkA) from Mycobacterium tuberculosis possesses an 80-residue disordered region (IDDPtkA ) of unknown function, located N-terminally to the well-folded kinase core domain. Here, we characterize the conformation of IDDPtkA under varying biophysical conditions and phosphorylation using NMR-spectroscopy. Our results confirm that the N-terminal domain of PtkA exists as an IDD at physiological pH. Furthermore, phosphorylation of IDDPtkA increases the activity of PtkA. Our findings will complement future approaches in understanding molecular mechanisms of key proteins in pathogenic virulence.
KW  - Mycobacterium tuberculosis
KW  - intrinsically disordered protein
KW  - nuclear magnetic resonance spectroscopy
KW  - protein denaturation
KW  - protein phosphorylation
KW  - protein tyrosine kinase
Y1  - 2018
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/51314
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-513140
N1  - Postprint, zuerst in: FEBS Letters, 592.2018, 7, S. 1233-1245. doi: 10.1002/1873-3468.13022, doi:10.1002/1873-3468.13022
Gefördert durch: European Union: Horizon 2020. Infrastructure for NMR, EM and X-rays for Translational Research, iNEXT, H2020 Grant # 653706
VL  - 592
IS  - 7
SP  - 1233
EP  - 1245
ER  -