The ubiquitin ligase SspH1 from <i>Salmonella</i> uses a modular and dynamic E3 domain to catalyze substrate ubiquitylation.

Cook, Matt; Delbecq, Scott P; Schweppe, Thomas P; Guttman, Miklos; Klevit, Rachel E; Brzovic, Peter S

The ubiquitin ligase SspH1 from Salmonella uses a modular and dynamic E3 domain to catalyze substrate ubiquitylation.

Cook, Matt; Delbecq, Scott P; Schweppe, Thomas P; Guttman, Miklos; Klevit, Rachel E; Brzovic, Peter S.

Afiliación

Cook M; From the Departments of Biochemistry and.
Delbecq SP; From the Departments of Biochemistry and.
Schweppe TP; From the Departments of Biochemistry and.
Guttman M; Medicinal Chemistry, University of Washington, Seattle, Washington 98195.
Klevit RE; From the Departments of Biochemistry and.
Brzovic PS; From the Departments of Biochemistry and brzovic@uw.edu.

J Biol Chem ; 294(3): 783-793, 2019 01 18.

Article en En | MEDLINE | ID: mdl-30459234

Asunto(s)

Proteínas Bacterianas/química; Salmonella/enzimología; Ubiquitina-Proteína Ligasas/química; Ubiquitinación; Sustitución de Aminoácidos; Proteínas Bacterianas/genética; Catálisis; Mutación Missense; Dominios Proteicos; Salmonella/genética; Ubiquitina-Proteína Ligasas/genética

Palabras clave

PKN1; Salmonella; SspH1; Ube2D; bacterial effector; bacterial pathogenesis; ubiquitin; ubiquitin ligase (E3 enzyme); ubiquitin transfer; ubiquitin-conjugating enzyme (E2 enzyme); ubiquitylation (ubiquitination)

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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Salmonella / Proteínas Bacterianas / Ubiquitina-Proteína Ligasas / Ubiquitinación Idioma: En Revista: J Biol Chem Año: 2019 Tipo del documento: Article Pais de publicación: Estados Unidos

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