The crystal structure of the catalytic domain of the ser/thr kinase PknA from M. tuberculosis shows an Src-like autoinhibited conformation.

Wagner, Tristan; Alexandre, Matthieu; Duran, Rosario; Barilone, Nathalie; Wehenkel, Annemarie; Alzari, Pedro M; Bellinzoni, Marco

Wagner, Tristan; Alexandre, Matthieu; Duran, Rosario; Barilone, Nathalie; Wehenkel, Annemarie; Alzari, Pedro M; Bellinzoni, Marco.

Affiliation

Wagner T; Institut Pasteur, Unité De Microbiologie Structurale, Paris, 75724, France; CNRS UMR 3528, Paris, 75724, France; Université Paris Diderot, Sorbonne Paris Cité, Microbiologie Structurale, Paris, 75724, France.

Proteins ; 83(5): 982-8, 2015 May.

Article in En | MEDLINE | ID: mdl-25586004

Subject(s)

Bacterial Proteins/chemistry; Mycobacterium tuberculosis/enzymology; Protein Serine-Threonine Kinases/chemistry; Amino Acid Sequence; Catalytic Domain; Crystallography, X-Ray; Enzyme Activation; Models, Molecular; Molecular Sequence Data; Phosphorylation; Protein Processing, Post-Translational; Protein Structure, Secondary

Key words

Mycobacterium tuberculosis; Ser/Thr phosphorylation; X-ray crystallography; autoinhibition; autophosphorylation; mass spectrometry

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Full text: 1 Collection: 01-internacional Health context: 3_ND Database: MEDLINE Main subject: Bacterial Proteins / Protein Serine-Threonine Kinases / Mycobacterium tuberculosis Language: En Journal: Proteins Year: 2015 Document type: Article

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