Structural insights into conformational switching in the copper metalloregulator CsoR from Streptomyces lividans

Acta Crystallographica. Section D, Biological Crystallography
Tatiana V PortoJonathan A R Worrall

Abstract

Copper-sensitive operon repressors (CsoRs) act to sense cuprous ions and bind them with a high affinity under copper stress in many bacteria. The binding of copper(I) leads to a conformational change in their homotetramer structure, causing disassembly of the operator DNA-CsoR complex and evoking a transcriptional response. Atomic-level structural insight into the conformational switching mechanism between the apo and metal-bound states is lacking. Here, a new X-ray crystal structure of the CsoR from Streptomyces lividans is reported and compared with a previously reported S. lividans CsoR X-ray structure crystallized under different conditions. Based on evidence from this new X-ray structure, it is revealed that the conformational switching between states centres on a concertina effect at the C-terminal end of each α2 helix in the homotetramer. This drives the Cys104 side chain, a copper(I)-ligating residue, into a position enabling copper(I) coordination and as a result disrupts the α2-helix geometry, leading to a compacting and twisting of the homotetramer structure. Strikingly, the conformational switching induces a redistribution of electrostatic surface potential on the tetrameric DNA-binding face, which in the copper(I)-...Continue Reading

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Citations

Nov 5, 2015·Dalton Transactions : an International Journal of Inorganic Chemistry·Tatiana V PortoJonathan A R Worrall
Jan 14, 2020·Acta Crystallographica. Section F, Structural Biology Communications·Chao LiCarrie M Wilmot
May 11, 2017·Essays in Biochemistry·Daiana A CapdevilaDavid P Giedroc
Jan 3, 2018·Metallomics : Integrated Biometal Science·Megan L StrawJonathan A R Worrall
Jun 30, 2019·Inorganic Chemistry·Hsin-Ting Huang, Michael J Maroney
Nov 11, 2021·Nucleic Acids Research·Joseph N FakhouryDavid P Giedroc

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