Abstract
AbstractEstablishing 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.
References
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- 1H 13C and15N chemical shift assignments for Bud31p are deposited with accession code BMRB 25439 and1H and113Cd chemical shift assignments for the cysteines and metals of Bud31p (113Cd)3are deposited with accession code BMRB 25440.
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Dates
Type | When |
---|---|
Created | 10 years, 6 months ago (Feb. 20, 2015, 2:27 p.m.) |
Deposited | 1 year, 10 months ago (Oct. 6, 2023, 3:53 p.m.) |
Indexed | 1 year ago (Aug. 4, 2024, 8:55 p.m.) |
Issued | 10 years, 6 months ago (Feb. 20, 2015) |
Published | 10 years, 6 months ago (Feb. 20, 2015) |
Published Online | 10 years, 6 months ago (Feb. 20, 2015) |
Published Print | 10 years, 4 months ago (April 13, 2015) |
@article{van_Roon_2015, title={113Cd NMR Experiments Reveal an Unusual Metal Cluster in the Solution Structure of the Yeast Splicing Protein Bud31p}, volume={54}, ISSN={1521-3773}, url={http://dx.doi.org/10.1002/anie.201412210}, DOI={10.1002/anie.201412210}, number={16}, journal={Angewandte Chemie International Edition}, publisher={Wiley}, author={van Roon, Anne‐Marie M. and Yang, Ji‐Chun and Mathieu, Daniel and Bermel, Wolfgang and Nagai, Kiyoshi and Neuhaus, David}, year={2015}, month=feb, pages={4861–4864} }