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

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

(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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