title: Structural insight into the Mycobacterium tuberculosis Rv0020c protein and its interaction with the PknB kinase.
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).
authors: CNRS UMR 5048, Centre de Biochimie Structurale, 29, rue de Navacelles 34090 Montpellier, France.
authors: Christian
authors: C
authors: Roumestand
authors: Jade
authors: J
authors: Leiba
authors: Nathalie
authors: N
authors: Galophe
authors: Emmanuel
authors: E
authors: Margeat
authors: André
authors: A
authors: Padilla
authors: Yannick
authors: Y
authors: Bessin
authors: Philippe
authors: P
authors: Barthe
authors: Virginie
authors: V
authors: Molle
authors: Martin
authors: M
authors: Cohen-Gonsaud
mesh_terms: D000409:Alanine / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D020134:Catalytic Domain; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D005454:Fluorescence Polarization; D009682:Magnetic Resonance Spectroscopy; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D016297:Mutagenesis, Site-Directed; D009169:Mycobacterium tuberculosis / Q000737:chemistry / Q000378:metabolism*; D010766:Phosphorylation; D010957:Plasmids / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding; D017510:Protein Folding; D025941:Protein Interaction Mapping; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity; D013912:Threonine / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D008565:Membrane Proteins; D011994:Recombinant Proteins; D013912:Threonine; C475060:PknB protein, Mycobacterium tuberculosis; D017346:Protein Serine-Threonine Kinases; D000409:Alanine