2QIF

Crystal structure of a metallochaperone with a tetranuclear Cu(I) cluster

Summary for 2QIF

• Entry DOI: 10.2210/pdb2qif/pdb
• Related: 1K0V 1P8G
• Descriptor: Copper chaperone copZ, COPPER (I) ION, ACETATE ION, ... (6 entities in total)
• Functional Keywords: tetranuclear cu(i) cluster, chaperone
• Biological source: Bacillus subtilis
• Cellular location: Cytoplasm: O32221
• Total number of polymer chains: 2
• Total formula weight: 15196.79

Authors

West, C.,Singleton, C.,Kihlken, M.A.,Le Brun, N.E.,Hemmings, A.M. (deposition date: 2007-07-04, release date: 2008-07-08, Last modification date: 2024-02-21)

Primary citation

Hearnshaw, S.,West, C.,Singleton, C.,Zhou, L.,Kihlken, M.A.,Strange, R.W.,Le Brun, N.E.,Hemmings, A.M.
A tetranuclear Cu(I) cluster in the metallochaperone protein CopZ.
Biochemistry, 48:9324-9326, 2009

PubMed 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 [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.

PubMed: 19746989
DOI: 10.1021/bi9011995

Experimental method

X-RAY DIFFRACTION (1.5 Å)