Your browser doesn't support javascript.
loading
Chemical shift assignments for S. cerevisiae Ubc13.
Putney, D Reid; Todd, Emily A; Berndsen, Christopher E; Wright, Nathan T.
Afiliación
  • Putney DR; Department of Chemistry and Biochemistry, James Madison University, 901 Carrier Dr., Harrisonburg, VA, 22807, USA.
  • Todd EA; Department of Chemistry and Biochemistry, James Madison University, 901 Carrier Dr., Harrisonburg, VA, 22807, USA.
  • Berndsen CE; Department of Chemistry and Biochemistry, James Madison University, 901 Carrier Dr., Harrisonburg, VA, 22807, USA.
  • Wright NT; Department of Chemistry and Biochemistry, James Madison University, 901 Carrier Dr., Harrisonburg, VA, 22807, USA. wrightnt@jmu.edu.
Biomol NMR Assign ; 9(2): 407-10, 2015 Oct.
Article en En | MEDLINE | ID: mdl-25947351
The ubiquitination pathway controls several human cellular processes, most notably protein degradation. Ubiquitin, a small signaling protein, is activated by the E1 activating enzyme, transferred to an E2 conjugating enzyme, and then attached to a target substrate through a process that can be facilitated by an E3 ligase enzyme. The enzymatic mechanism of ubiquitin transfer from the E2 conjugating enzyme onto substrate is not clear. The highly conserved HPN motif in E2 catalytic domains is generally thought to help stabilize an oxyanion intermediate formed during ubiquitin transfer. However recent work suggests this motif is instead involved in a structural, non-enzymatic role. As a platform to better understand the E2 catalyzed ubiquitin transfer mechanism, we determined the chemical shift assignments of S. cerevisiae E2 enzyme Ubc13.
Asunto(s)
Palabras clave

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Saccharomyces cerevisiae / Resonancia Magnética Nuclear Biomolecular / Proteínas de Saccharomyces cerevisiae / Enzimas Ubiquitina-Conjugadoras Idioma: En Revista: Biomol NMR Assign Asunto de la revista: BIOLOGIA MOLECULAR / MEDICINA NUCLEAR Año: 2015 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Países Bajos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Saccharomyces cerevisiae / Resonancia Magnética Nuclear Biomolecular / Proteínas de Saccharomyces cerevisiae / Enzimas Ubiquitina-Conjugadoras Idioma: En Revista: Biomol NMR Assign Asunto de la revista: BIOLOGIA MOLECULAR / MEDICINA NUCLEAR Año: 2015 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Países Bajos