¹¹³Cd NMR experiments reveal an unusual metal cluster in the solution structure of the yeast splicing protein Bud31p.
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 Zn3Cys9 cluster, demonstrating that recent hardware developments make this approach feasible for significantly larger systems.
['van Roon|Anne-Marie M|AM|', 'Yang|Ji-Chun|JC|', 'Mathieu|Daniel|D|', 'Bermel|Wolfgang|W|', 'Nagai|Kiyoshi|K|', 'Neuhaus|David|D|']
D002104:Cadmium D007554:Isotopes D009682:Magnetic Resonance Spectroscopy D008670:Metals D011485:Protein Binding D017434:Protein Structure, Tertiary D012441:Saccharomyces cerevisiae D029701:Saccharomyces cerevisiae Proteins D012996:Solutions D055672:Static Electricity D015032:Zinc
metal clusters NMR spectroscopy heteronuclear correlation structure elucidation zinc finger proteins