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113 Cd NMR Experiments Reveal an Unusual Metal Cluster in the Solution Structure of the Yeast Splicing Protein Bud31p
Author(s) -
van Roon AnneMarie M.,
Yang JiChun,
Mathieu Daniel,
Bermel Wolfgang,
Nagai Kiyoshi,
Neuhaus David
Publication year - 2015
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201412210
Subject(s) - nuclear magnetic resonance spectroscopy , chemistry , yeast , zinc , crystallography , cluster (spacecraft) , rna splicing , protein structure , structural biology , spectroscopy , residue (chemistry) , metal ions in aqueous solution , metal , stereochemistry , biochemistry , physics , organic chemistry , gene , rna , computer science , programming language , quantum mechanics
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.