Structural Basis of Low-Affinity Nickel Binding to the Nickel-Responsive Transcription Factor NikR from Escherichia coli
Escherichia coli NikR regulates cellular nickel uptake by binding to the nik operon in the presence of nickel and blocking transcription of genes encoding the nickel uptake transporter. NikR has two binding affinities for the nik operon: a nanomolar dissociation constant with stoichiometric nickel a...
Main Authors: | Phillips, Christine M., Schreiter, Eric R., Stultz, Collin M., Drennan, Catherine L. |
---|---|
Other Authors: | Massachusetts Institute of Technology. Department of Chemistry |
Format: | Article |
Language: | en_US |
Published: |
American Chemical Society
2011
|
Online Access: | http://hdl.handle.net/1721.1/64719 https://orcid.org/0000-0001-5486-2755 https://orcid.org/0000-0002-3415-242X |
Similar Items
-
Physical Basis of Metal-Binding Specificity in Escherichia coli NikR
by: Phillips, Christine M., et al.
Published: (2013) -
Relating metal binding to DNA binding in the nickel regulatory protein NikR
by: Phillips, Christine M. (Christine Marie)
Published: (2010) -
Crystallographic studies of the metal-responsive transcription factor NikR
by: Schreiter, Eric R. (Eric Robert)
Published: (2006) -
Cellular uptake of nickel by NikR is regulated by phase separation
by: Kaiming Cao, et al.
Published: (2023-06-01) -
Potassium is critical for the Ni(II)-responsive DNA-binding activity of Escherichia coli NikR.
by: Wang, S, et al.
Published: (2010)