NMR characterization of a Cu(i)-bound peptide model of copper metallochaperones: Insights on the role of methionine

Michal S. Shoshan; Deborah E. Shalev; Wencke Adriaens; Maarten Merkx; Tilman M. Hackeng; Edit Y. Tshuva

doi:10.1039/c1cc11600b

NMR characterization of a Cu(i)-bound peptide model of copper metallochaperones: Insights on the role of methionine

Michal S. Shoshan
, Deborah E. Shalev
, Wencke Adriaens
, Maarten Merkx
, Tilman M. Hackeng
, Edit Y. Tshuva

Research output: Contribution to journal › Article › peer-review

8 Scopus citations

Abstract

The first NMR structure of a Cu(i)-bound metallochaperone model with the conserved sequence MT/HCXXC revealed that at pH ∼3.0 and ∼6.8 Cu(i) binds through one Cys and the Met rather than the two Cys residues, differently than at pH ∼8.5. This suggests a possible role of Met in metal transport.

Original language	English
Pages (from-to)	6407-6409
Number of pages	3
Journal	Chemical Communications
Volume	47
Issue number	22
DOIs	https://doi.org/10.1039/c1cc11600b
State	Published - 14 Jun 2011

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abstract = "The first NMR structure of a Cu(i)-bound metallochaperone model with the conserved sequence MT/HCXXC revealed that at pH ∼3.0 and ∼6.8 Cu(i) binds through one Cys and the Met rather than the two Cys residues, differently than at pH ∼8.5. This suggests a possible role of Met in metal transport.",

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T2 - Insights on the role of methionine

AU - Shoshan, Michal S.

AU - Shalev, Deborah E.

AU - Adriaens, Wencke

AU - Merkx, Maarten

AU - Hackeng, Tilman M.

AU - Tshuva, Edit Y.

PY - 2011/6/14

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AB - The first NMR structure of a Cu(i)-bound metallochaperone model with the conserved sequence MT/HCXXC revealed that at pH ∼3.0 and ∼6.8 Cu(i) binds through one Cys and the Met rather than the two Cys residues, differently than at pH ∼8.5. This suggests a possible role of Met in metal transport.

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NMR characterization of a Cu(i)-bound peptide model of copper metallochaperones: Insights on the role of methionine

Abstract

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