5NQO

CU(I)-CSP3 (COPPER STORAGE PROTEIN 3) FROM METHYLOSINUS

Summary for 5NQO

• Entry DOI: 10.2210/pdb5nqo/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: 15649.04

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

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: 28504850
DOI: 10.1002/anie.201703107

Experimental method

X-RAY DIFFRACTION (1.15 Å)