Structural highlights
Function
BUD31_YEAST Involved in pre-mRNA splicing. Important for bud site selection.
Publication Abstract from PubMed
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.
Cd NMR Experiments Reveal an Unusual Metal Cluster in the Solution Structure of the Yeast Splicing Protein Bud31p.,van Roon AM, Yang JC, Mathieu D, Bermel W, Nagai K, Neuhaus D Angew Chem Int Ed Engl. 2015 Feb 20. doi: 10.1002/anie.201412210. PMID:25703931[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ van Roon AM, Yang JC, Mathieu D, Bermel W, Nagai K, Neuhaus D. 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. doi: 10.1002/anie.201412210. PMID:25703931 doi:http://dx.doi.org/10.1002/anie.201412210