The domain architecture of PtkA, the first tyrosine kinase from <i>Mycobacterium tuberculosis</i>, differs from the conventional kinase architecture.

Niesteruk, Anna; Jonker, Hendrik R A; Richter, Christian; Linhard, Verena; Sreeramulu, Sridhar; Schwalbe, Harald

The domain architecture of PtkA, the first tyrosine kinase from Mycobacterium tuberculosis, differs from the conventional kinase architecture.

Niesteruk, Anna; Jonker, Hendrik R A; Richter, Christian; Linhard, Verena; Sreeramulu, Sridhar; Schwalbe, Harald.

Afiliação

Niesteruk A; From the Institute for Organic Chemistry and Chemical Biology, Centre for Biomolecular Magnetic Resonance (BMRZ), Goethe-University Frankfurt am Main, Max-von-Laue-Strasse 7, D-60438 Frankfurt am Main, Germany.
Jonker HRA; From the Institute for Organic Chemistry and Chemical Biology, Centre for Biomolecular Magnetic Resonance (BMRZ), Goethe-University Frankfurt am Main, Max-von-Laue-Strasse 7, D-60438 Frankfurt am Main, Germany.
Richter C; From the Institute for Organic Chemistry and Chemical Biology, Centre for Biomolecular Magnetic Resonance (BMRZ), Goethe-University Frankfurt am Main, Max-von-Laue-Strasse 7, D-60438 Frankfurt am Main, Germany.
Linhard V; From the Institute for Organic Chemistry and Chemical Biology, Centre for Biomolecular Magnetic Resonance (BMRZ), Goethe-University Frankfurt am Main, Max-von-Laue-Strasse 7, D-60438 Frankfurt am Main, Germany.
Sreeramulu S; From the Institute for Organic Chemistry and Chemical Biology, Centre for Biomolecular Magnetic Resonance (BMRZ), Goethe-University Frankfurt am Main, Max-von-Laue-Strasse 7, D-60438 Frankfurt am Main, Germany.
Schwalbe H; From the Institute for Organic Chemistry and Chemical Biology, Centre for Biomolecular Magnetic Resonance (BMRZ), Goethe-University Frankfurt am Main, Max-von-Laue-Strasse 7, D-60438 Frankfurt am Main, Germany schwalbe@nmr.uni-frankfurt.de.

J Biol Chem ; 293(30): 11823-11836, 2018 07 27.

Article em En | MEDLINE | ID: mdl-29884774

Assuntos

Proteínas de Bactérias/química; Mycobacterium tuberculosis/enzimologia; Proteínas Tirosina Quinases/química; Proteínas de Bactérias/metabolismo; Humanos; Ligação de Hidrogênio; Modelos Moleculares; Mycobacterium tuberculosis/química; Mycobacterium tuberculosis/metabolismo; Ressonância Magnética Nuclear Biomolecular; Fosforilação; Conformação Proteica; Proteínas Tirosina Fosfatases/metabolismo; Proteínas Tirosina Quinases/metabolismo; Tuberculose/microbiologia

Palavras-chave

Mycobacterium tuberculosis; autophosphorylation; bacterial protein kinase; bacterial protein phosphatase; intrinsically disordered protein; low-molecular-weight protein tyrosine phosphatase A; nuclear magnetic resonance (NMR); protein dynamic; protein tyrosine kinase A; reversible phosphorylation

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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas de Bactérias / Proteínas Tirosina Quinases / Mycobacterium tuberculosis Limite: Humans Idioma: En Ano de publicação: 2018 Tipo de documento: Article

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