(113) Cd NMR Experiments Reveal an Unusual Metal Cluster in the Solution Structure of the Yeast Splicing Protein Bud31p.
Angew Chem Int Ed Engl. 2015 Feb 20;
Authors: van Roon AM, Yang JC, Mathieu D, Bermel W, Nagai K, Neuhaus D
Abstract
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 Zn3 Cys9 cluster, demonstrating that recent hardware developments make this approach feasible for significantly larger systems.
PMID: 25703931 [PubMed - as supplied by publisher]
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(113) Cd NMR Experiments Reveal an Unusual Metal Cluster in the Solution Structure of the Yeast Splicing Protein Bud31p.
Linear Mode
