5fig

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

spinqualitylabelsall models 5fig, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5fig is a 6 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function YHJQ_BACSU Publication Abstract from PubMed 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) x 10(17) M(-1) 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. Bacterial cytosolic proteins with a high capacity for Cu(I) that protect against copper toxicity.,Vita N, Landolfi G, Basle A, Platsaki S, Lee J, Waldron KJ, Dennison C Sci Rep. 2016 Dec 19;6:39065. doi: 10.1038/srep39065. PMID:27991525 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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