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

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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...

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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:
Zuschriften
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4954022/
https://www.ncbi.nlm.nih.gov/pubmed/27478262
http://dx.doi.org/10.1002/ange.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.

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