5FIG

APO-CSP3 (COPPER STORAGE PROTEIN 3) FROM BACILLUS SUBTILIS

Summary for 5FIG

• Entry DOI: 10.2210/pdb5fig/pdb
• Related: 5ARM 5ARN
• Descriptor: CSP3 (2 entities in total)
• Functional Keywords: copper-binding protein, copper storage, bacillus subtilis
• Biological source: BACILLUS SUBTILIS
• Total number of polymer chains: 6
• Total formula weight: 71122.55

Authors

Vita, N.,Landolfi, G.,Basle, A.,Platsaki, S.,Waldron, K.,Dennison, C. (deposition date: 2015-09-25, release date: 2016-10-12, Last modification date: 2024-11-20)

Primary citation

Vita, N.,Landolfi, G.,Basle, A.,Platsaki, S.,Lee, J.,Waldron, K.J.,Dennison, C.
Bacterial cytosolic proteins with a high capacity for Cu(I) that protect against copper toxicity.
Sci Rep, 6:39065-39065, 2016

PubMed Abstract: Bacteria are thought to avoid using the essential metal ion copper in their cytosol due to its toxicity. Herein we characterize Csp3, the cytosolic member of a new family of bacterial copper storage proteins from Methylosinus trichosporium OB3b and Bacillus subtilis. These tetrameric proteins possess a large number of Cys residues that point into the cores of their four-helix bundle monomers. The Csp3 tetramers can bind a maximum of approximately 80 Cu(I) ions, mainly via thiolate groups, with average affinities in the (1-2) × 10 M range. Cu(I) removal from these Csp3s by higher affinity potential physiological partners and small-molecule ligands is very slow, which is unexpected for a metal-storage protein. In vivo data demonstrate that Csp3s prevent toxicity caused by the presence of excess copper. Furthermore, bacteria expressing Csp3 accumulate copper and are able to safely maintain large quantities of this metal ion in their cytosol. This suggests a requirement for storing copper in this compartment of Csp3-producing bacteria.

PubMed: 27991525
DOI: 10.1038/srep39065

Experimental method

X-RAY DIFFRACTION (1.7 Å)