5NQM
CU(I)-CSP3 (COPPER STORAGE PROTEIN 3) FROM METHYLOSINUS
Summary for 5NQM
| Entry DOI | 10.2210/pdb5nqm/pdb |
| Descriptor | CSP3, COPPER (I) ION, SODIUM ION, ... (4 entities in total) |
| Functional Keywords | copper-binding protein, methane oxidation, copper storage, methanotrophs, particulate methane monooxygenase |
| Biological source | Methylosinus trichosporium OB3b |
| Total number of polymer chains | 1 |
| Total formula weight | 14822.94 |
| Authors | Basle, A.,Platsaki, S.,Dennison, C. (deposition date: 2017-04-20, release date: 2017-05-31, Last modification date: 2024-01-17) |
| Primary citation | Basle, A.,Platsaki, S.,Dennison, C. Visualizing Biological Copper Storage: The Importance of Thiolate-Coordinated Tetranuclear Clusters. Angew. Chem. Int. Ed. Engl., 56:8697-8700, 2017 Cited by PubMed Abstract: Bacteria possess cytosolic proteins (Csp3s) capable of binding large quantities of copper and preventing toxicity. Crystal structures of a Csp3 plus increasing amounts of Cu provide atomic-level information about how a storage protein loads with metal ions. Many more sites are occupied than Cu equiv added, with binding by twelve central sites dominating. These can form [Cu (S-Cys) ] intermediates leading to [Cu (S-Cys) ] , [Cu (S-Cys) ] , and [Cu (S-Cys) (O-Asn)] clusters. Construction of the five Cu sites at the opening of the bundle lags behind the main core, and the two least accessible sites at the opposite end of the bundle are occupied last. Facile Cu cluster formation, reminiscent of that for inorganic complexes with organothiolate ligands, is largely avoided in biology but is used by proteins that store copper in the cytosol of prokaryotes and eukaryotes, where this reactivity is also key to toxicity. PubMed: 28504850DOI: 10.1002/anie.201703107 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.59 Å) |
Structure validation
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