A tetranuclear Cu(I) cluster in the metallochaperone protein CopZ

Stephen Hearnshaw; Claire West; Chloe Singleton; Liang Zhou; Margaret A. Kihlken; Richard W. Strange; Nick E. Le Brun; Andrew M. Hemmings

doi:10.1021/bi9011995

A tetranuclear Cu(I) cluster in the metallochaperone protein CopZ

Stephen Hearnshaw, Claire West, Chloe Singleton, Liang Zhou, Margaret A. Kihlken, Richard W. Strange, Nick E. Le Brun, Andrew M. Hemmings

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

30 Citations (Scopus)

Abstract

Copper trafficking proteins and copper-sensitive regulators are often found to be able to bind multiple Cu(I) ions in the form of Cu(I) clusters. We have determined the high-resolution X-ray crystal structure of an Atx1-like copper chaperone protein from Bacillus subtilis containing a novel tetranuclear Cu(I) cluster. The identities and oxidation states of the cluster ions were established unambiguously by refinement of X-ray energy-dependent anomalous scattering factors. The [Cu4(S-Cys)4(N-His)2] cluster geometry provides new structural insights into not only the binding of multiple cuprous ions by metallochaperones but also protein-associated tetranuclear Cu(I) clusters, including those found in eukaryotic copper-responsive transcription factors.

Original language	English
Pages (from-to)	9324-9326
Number of pages	3
Journal	Biochemistry
Volume	48
Issue number	40
DOIs	https://doi.org/10.1021/bi9011995
Publication status	Published - 11 Sep 2009

Access to Document

10.1021/bi9011995

Cite this

@article{76ab9e1bf6ff4802818be53596b40ef2,

title = "A tetranuclear Cu(I) cluster in the metallochaperone protein CopZ",

abstract = "Copper trafficking proteins and copper-sensitive regulators are often found to be able to bind multiple Cu(I) ions in the form of Cu(I) clusters. We have determined the high-resolution X-ray crystal structure of an Atx1-like copper chaperone protein from Bacillus subtilis containing a novel tetranuclear Cu(I) cluster. The identities and oxidation states of the cluster ions were established unambiguously by refinement of X-ray energy-dependent anomalous scattering factors. The [Cu4(S-Cys)4(N-His)2] cluster geometry provides new structural insights into not only the binding of multiple cuprous ions by metallochaperones but also protein-associated tetranuclear Cu(I) clusters, including those found in eukaryotic copper-responsive transcription factors.",

author = "Stephen Hearnshaw and Claire West and Chloe Singleton and Liang Zhou and Kihlken, {Margaret A.} and Strange, {Richard W.} and {Le Brun}, {Nick E.} and Hemmings, {Andrew M.}",

year = "2009",

month = sep,

day = "11",

doi = "10.1021/bi9011995",

language = "English",

volume = "48",

pages = "9324--9326",

journal = "Biochemistry",

issn = "0006-2960",

publisher = "American Chemical Society",

number = "40",

}

TY - JOUR

T1 - A tetranuclear Cu(I) cluster in the metallochaperone protein CopZ

AU - Hearnshaw, Stephen

AU - West, Claire

AU - Singleton, Chloe

AU - Zhou, Liang

AU - Kihlken, Margaret A.

AU - Strange, Richard W.

AU - Le Brun, Nick E.

AU - Hemmings, Andrew M.

PY - 2009/9/11

Y1 - 2009/9/11

N2 - Copper trafficking proteins and copper-sensitive regulators are often found to be able to bind multiple Cu(I) ions in the form of Cu(I) clusters. We have determined the high-resolution X-ray crystal structure of an Atx1-like copper chaperone protein from Bacillus subtilis containing a novel tetranuclear Cu(I) cluster. The identities and oxidation states of the cluster ions were established unambiguously by refinement of X-ray energy-dependent anomalous scattering factors. The [Cu4(S-Cys)4(N-His)2] cluster geometry provides new structural insights into not only the binding of multiple cuprous ions by metallochaperones but also protein-associated tetranuclear Cu(I) clusters, including those found in eukaryotic copper-responsive transcription factors.

AB - Copper trafficking proteins and copper-sensitive regulators are often found to be able to bind multiple Cu(I) ions in the form of Cu(I) clusters. We have determined the high-resolution X-ray crystal structure of an Atx1-like copper chaperone protein from Bacillus subtilis containing a novel tetranuclear Cu(I) cluster. The identities and oxidation states of the cluster ions were established unambiguously by refinement of X-ray energy-dependent anomalous scattering factors. The [Cu4(S-Cys)4(N-His)2] cluster geometry provides new structural insights into not only the binding of multiple cuprous ions by metallochaperones but also protein-associated tetranuclear Cu(I) clusters, including those found in eukaryotic copper-responsive transcription factors.

U2 - 10.1021/bi9011995

DO - 10.1021/bi9011995

M3 - Article

VL - 48

SP - 9324

EP - 9326

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 40

ER -