4M1P

Crystal structure of the copper-sensing repressor CsoR with Cu(I) from Geobacillus thermodenitrificans NG80-2

Summary for 4M1P

• Entry DOI: 10.2210/pdb4m1p/pdb
• Related: 4ADZ
• Descriptor: Copper-sensitive operon repressor (CsoR), COPPER (I) ION, SODIUM ION, ... (4 entities in total)
• Functional Keywords: cu(i)-sensing transcriptional repressor, cu(i) binding, transcription repressor
• Biological source: Geobacillus thermodenitrificans
• Total number of polymer chains: 1
• Total formula weight: 12056.44

Authors

Chang, F.,Dann III, C.E.,Giedroc, D.P. (deposition date: 2013-08-03, release date: 2014-05-21, Last modification date: 2023-09-20)

Primary citation

Chang, F.M.,Coyne, H.J.,Cubillas, C.,Vinuesa, P.,Fang, X.,Ma, Z.,Ma, D.,Helmann, J.D.,Garcia-de los Santos, A.,Wang, Y.X.,Dann, C.E.,Giedroc, D.P.
Cu(I)-mediated allosteric switching in a copper-sensing operon repressor (CsoR).
J.Biol.Chem., 289:19204-19217, 2014

PubMed Abstract: The copper-sensing operon repressor (CsoR) is representative of a major Cu(I)-sensing family of bacterial metalloregulatory proteins that has evolved to prevent cytoplasmic copper toxicity. It is unknown how Cu(I) binding to tetrameric CsoRs mediates transcriptional derepression of copper resistance genes. A phylogenetic analysis of 227 DUF156 protein members, including biochemically or structurally characterized CsoR/RcnR repressors, reveals that Geobacillus thermodenitrificans (Gt) CsoR characterized here is representative of CsoRs from pathogenic bacilli Listeria monocytogenes and Bacillus anthracis. The 2.56 Å structure of Cu(I)-bound Gt CsoR reveals that Cu(I) binding induces a kink in the α2-helix between two conserved copper-ligating residues and folds an N-terminal tail (residues 12-19) over the Cu(I) binding site. NMR studies of Gt CsoR reveal that this tail is flexible in the apo-state with these dynamics quenched upon Cu(I) binding. Small angle x-ray scattering experiments on an N-terminally truncated Gt CsoR (Δ2-10) reveal that the Cu(I)-bound tetramer is hydrodynamically more compact than is the apo-state. The implications of these findings for the allosteric mechanisms of other CsoR/RcnR repressors are discussed.

PubMed: 24831014
DOI: 10.1074/jbc.M114.556704

Experimental method

X-RAY DIFFRACTION (2.564 Å)