title: 113Cd NMR Experiments Reveal an Unusual Metal Cluster in the Solution Structure of the Yeast Splicing Protein Bud31p.
abstract: Establishing the binding topology of structural zinc ions in proteins is an essential part of their structure determination by NMR spectroscopy. Using113Cd NMR experiments with113Cd-substituted samples is a useful approach but has previously been limited mainly to very small protein domains. Here we used113Cd NMR spectroscopy during structure determination of Bud31p, a 157-residue yeast protein containing an unusual Zn3Cys9cluster, demonstrating that recent hardware developments make this approach feasible for significantly larger systems.
authors.affiliation: MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH (UK).
authors.forename: Anne-Marie M
authors.initials: AM
authors.lastname: van Roon
authors.affiliation: MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH (UK).
authors.forename: Ji-Chun
authors.initials: JC
authors.lastname: Yang
authors.affiliation: Bruker BioSpin GmbH, Silberstreifen, 76287 Rheinstetten (Germany).
authors.forename: Daniel
authors.initials: D
authors.lastname: Mathieu
authors.affiliation: Bruker BioSpin GmbH, Silberstreifen, 76287 Rheinstetten (Germany).
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Bermel
authors.affiliation: MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH (UK).
authors.forename: Kiyoshi
authors.initials: K
authors.lastname: Nagai
authors.affiliation: MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH (UK).
authors.forename: David
authors.initials: D
authors.lastname: Neuhaus
keywords: Heteronukleare Korrelation; Metallcluster; NMR‐Spektroskopie; Strukturaufklärung; Zinkfingerproteine