A tetranuclear Cu(I) cluster in the metallochaperone protein CopZ.
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 [Cu(4)(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.
Hearnshaw
Stephen
S
Centre for Molecular and Structural Biochemistry, School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK.
West
Claire
C
Singleton
Chloe
C
Zhou
Liang
L
Kihlken
Margaret A
MA
Strange
Richard W
RW
Le Brun
Nick E
NE
Hemmings
Andrew M
AM
D001412:Bacillus subtilis / Q000737:chemistry / Q000502:physiology; D001426:Bacterial Proteins / Q000737:chemistry* / Q000502:physiology; D003300:Copper / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D019281:Dimerization; D008667:Metalloproteins / Q000737:chemistry* / Q000502:physiology; D018832:Molecular Chaperones / Q000737:chemistry* / Q000502:physiology
D001426:Bacterial Proteins; D008667:Metalloproteins; D018832:Molecular Chaperones; D003300:Copper