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4BPY

Crystal structure of the C90A mutant of the Sco copper chaperone protein from Streptomyces lividans

Summary for 4BPY
Entry DOI10.2210/pdb4bpy/pdb
DescriptorSCO PROTEIN (2 entities in total)
Functional Keywordscopper homeostasis, chaperone, homeostasis
Biological sourceSTREPTOMYCES LIVIDANS
Total number of polymer chains1
Total formula weight19059.48
Authors
Blundell, K.L.I.M.,Hough, M.A.,Worrall, J.A.R. (deposition date: 2013-05-29, release date: 2014-03-05, Last modification date: 2024-11-13)
Primary citationBlundell, K.L.I.M.,Hough, M.A.,Vijgenboom, E.,Worrall, J.A.R.
Structural and Mechanistic Insights Into an Extracytoplasmic Copper Trafficking Pathway in Streptomyces Lividans.
Biochem.J., 459:525-, 2014
Cited by
PubMed Abstract: In Streptomyces lividans an extracytoplasmic copper-binding Sco protein plays a role in two unlinked processes: (i) initiating a morphological development switch and (ii) facilitating the co-factoring of the CuA domain of CcO (cytochrome c oxidase). How Sco obtains copper once secreted to the extracytoplasmic environment is unknown. In the present paper we report on a protein possessing an HX₆MX₂₁HXM motif that binds a single cuprous ion with subfemtomolar affinity. High-resolution X-ray structures of this extracytoplasmic copper chaperone-like protein (ECuC) in the apo- and Cu(I)-bound states reveal that the latter possesses a surface-accessible cuprous-ion-binding site located in a dish-shaped region of β-sheet structure. A cuprous ion is transferred under a favourable thermodynamic gradient from ECuC to Sco with no back transfer occurring. The ionization properties of the cysteine residues in the Cys⁸⁶xxxCys⁹⁰ copper-binding motif of Sco, together with their positional locations identified from an X-ray structure of Sco, suggests a role for Cys⁸⁶ in initiating an inter-complex ligand-exchange reaction with Cu(I)-ECuC. Generation of the genetic knockouts, Δsco, Δecuc and Δsco/ecuc, and subsequent in vivo assays lend support to the existence of a branched extracytoplasmic copper-trafficking pathway in S. lividans. One branch requires both Sco and to a certain extent ECuC to cofactor the CuA domain, whereas the other uses only Sco to deliver copper to a cuproenzyme to initiate morphological development.
PubMed: 24548299
DOI: 10.1042/BJ20140017
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.4 Å)
Structure validation

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