113Cd NMR Experiments Reveal an Unusual Metal Cluster in the Solution Structure of the Yeast Splicing Protein Bud31p1. Issue 16 (20th February 2015)

• Record Type: Journal Article
• Authors: van Roon, Anne‐Marie M.; Yang, Ji‐Chun; Mathieu, Daniel; Bermel, Wolfgang; Nagai, Kiyoshi; Neuhaus, David
• Is Part Of: Angewandte Chemie international edition. Volume 54:Issue 16(2015)
• Page Start: 4861
• Page End: 4864
• Publication Date: 2015-02-20
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201412210
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>Establishing the binding topology of structural zinc ions in proteins is an essential part of their structure determination by NMR spectroscopy. Using ¹¹³Cd NMR experiments with ¹¹³Cd‐substituted samples is a useful approach but has previously been limited mainly to very small protein domains. Here we used ¹¹³Cd NMR spectroscopy during structure determination of Bud31p, a 157‐residue yeast protein containing an unusual Zn₃Cys₉ cluster, demonstrating that recent hardware developments make this approach feasible for significantly larger systems.</p> </abstract>