(113)Cd NMR Experiments Reveal an Unusual Metal Cluster in the Solution Structure of the Yeast Splicing Protein Bud31p**

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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. H...

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Detalles Bibliográficos
Autores principales: van Roon, Anne-Marie M, Yang, Ji-Chun, Mathieu, Daniel, Bermel, Wolfgang, Nagai, Kiyoshi, Neuhaus, David
Formato: Online Artículo Texto
Lenguaje:English
Publicado: WILEY-VCH Verlag 2015
Materias:
Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4471582/
https://www.ncbi.nlm.nih.gov/pubmed/25703931
http://dx.doi.org/10.1002/anie.201412210
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author van Roon, Anne-Marie M
Yang, Ji-Chun
Mathieu, Daniel
Bermel, Wolfgang
Nagai, Kiyoshi
Neuhaus, David
author_facet van Roon, Anne-Marie M
Yang, Ji-Chun
Mathieu, Daniel
Bermel, Wolfgang
Nagai, Kiyoshi
Neuhaus, David
author_sort van Roon, Anne-Marie M
collection PubMed
description 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 Zn(3)Cys(9) cluster, demonstrating that recent hardware developments make this approach feasible for significantly larger systems.
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spelling pubmed-44715822015-06-23 (113)Cd NMR Experiments Reveal an Unusual Metal Cluster in the Solution Structure of the Yeast Splicing Protein Bud31p** van Roon, Anne-Marie M Yang, Ji-Chun Mathieu, Daniel Bermel, Wolfgang Nagai, Kiyoshi Neuhaus, David Angew Chem Int Ed Engl Communications 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 Zn(3)Cys(9) cluster, demonstrating that recent hardware developments make this approach feasible for significantly larger systems. WILEY-VCH Verlag 2015-04-13 2015-02-20 /pmc/articles/PMC4471582/ /pubmed/25703931 http://dx.doi.org/10.1002/anie.201412210 Text en © 2015 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. http://creativecommons.org/licenses/by/3.0/ This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Communications
van Roon, Anne-Marie M
Yang, Ji-Chun
Mathieu, Daniel
Bermel, Wolfgang
Nagai, Kiyoshi
Neuhaus, David
(113)Cd NMR Experiments Reveal an Unusual Metal Cluster in the Solution Structure of the Yeast Splicing Protein Bud31p**
title (113)Cd NMR Experiments Reveal an Unusual Metal Cluster in the Solution Structure of the Yeast Splicing Protein Bud31p**
title_full (113)Cd NMR Experiments Reveal an Unusual Metal Cluster in the Solution Structure of the Yeast Splicing Protein Bud31p**
title_fullStr (113)Cd NMR Experiments Reveal an Unusual Metal Cluster in the Solution Structure of the Yeast Splicing Protein Bud31p**
title_full_unstemmed (113)Cd NMR Experiments Reveal an Unusual Metal Cluster in the Solution Structure of the Yeast Splicing Protein Bud31p**
title_short (113)Cd NMR Experiments Reveal an Unusual Metal Cluster in the Solution Structure of the Yeast Splicing Protein Bud31p**
title_sort (113)cd nmr experiments reveal an unusual metal cluster in the solution structure of the yeast splicing protein bud31p**
topic Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4471582/
https://www.ncbi.nlm.nih.gov/pubmed/25703931
http://dx.doi.org/10.1002/anie.201412210
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