Back to Search
Start Over
Structural insight into the Mycobacterium tuberculosis Rv0020c protein and its interaction with the PknB kinase.
- Source :
-
Structure (London, England : 1993) [Structure] 2011 Oct 12; Vol. 19 (10), pp. 1525-34. - Publication Year :
- 2011
-
Abstract
- The protein Rv0020c from Mycobacterium tuberculosis, also called FhaA, is one of the major substrates of the essential Ser/Thr protein kinase (STPK) PknB. The protein is composed of three domains and is phosphorylated on a unique site in its N terminus. We solved the solution structure of both N- and C-terminal domains and demonstrated that the approximately 300 amino acids of the intermediate domain are not folded. We present evidence that the FHA, a phosphospecific binding domain, of Rv0020c does not interact with the phosphorylated catalytic domains of PknB, but with the phosphorylated juxtamembrane domain that links the catalytic domain to the mycobacterial membrane. We also demonstrated that the degree and the pattern of phosphorylation of this juxtamembrane domain modulates the affinity of the substrate (Rv0020c) toward its kinase (PknB).<br /> (Copyright © 2011 Elsevier Ltd. All rights reserved.)
- Subjects :
- Alanine metabolism
Bacterial Proteins chemistry
Binding Sites
Catalytic Domain
Cloning, Molecular
Escherichia coli genetics
Escherichia coli metabolism
Fluorescence Polarization
Magnetic Resonance Spectroscopy
Membrane Proteins chemistry
Membrane Proteins metabolism
Mutagenesis, Site-Directed
Mycobacterium tuberculosis chemistry
Phosphorylation
Plasmids genetics
Plasmids metabolism
Protein Binding
Protein Folding
Protein Interaction Mapping
Protein Serine-Threonine Kinases chemistry
Recombinant Proteins chemistry
Recombinant Proteins metabolism
Substrate Specificity
Threonine metabolism
Bacterial Proteins metabolism
Mycobacterium tuberculosis metabolism
Protein Serine-Threonine Kinases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1878-4186
- Volume :
- 19
- Issue :
- 10
- Database :
- MEDLINE
- Journal :
- Structure (London, England : 1993)
- Publication Type :
- Academic Journal
- Accession number :
- 22000520
- Full Text :
- https://doi.org/10.1016/j.str.2011.07.011