(113)Cd NMR Experiments Reveal an Unusual Metal Cluster in the Solution Structure of the Yeast Splicing Protein Bud31p**

Mostrar otras versiones (1)

Establishing the binding topology of structural zinc ions in proteins is an essential part of their structure determination by NMR spectroscopy. Using (113)Cd NMR experiments with (113)Cd-substituted samples is a useful approach but has previously been limited mainly to very small protein domains. H...

Descripción completa

Detalles Bibliográficos
Autores principales: van Roon, Anne-Marie M, Yang, Ji-Chun, Mathieu, Daniel, Bermel, Wolfgang, Nagai, Kiyoshi, Neuhaus, David
Formato: Online Artículo Texto
Lenguaje:English
Publicado: WILEY-VCH Verlag 2015
Materias:
Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4471582/
https://www.ncbi.nlm.nih.gov/pubmed/25703931
http://dx.doi.org/10.1002/anie.201412210
Descripción
Sumario:Establishing the binding topology of structural zinc ions in proteins is an essential part of their structure determination by NMR spectroscopy. Using (113)Cd NMR experiments with (113)Cd-substituted samples is a useful approach but has previously been limited mainly to very small protein domains. Here we used (113)Cd NMR spectroscopy during structure determination of Bud31p, a 157-residue yeast protein containing an unusual Zn(3)Cys(9) cluster, demonstrating that recent hardware developments make this approach feasible for significantly larger systems.

Ejemplares similares