3BKF

Zinc-bound C-terminal Domain of NikR

Summary for 3BKF

• Entry DOI: 10.2210/pdb3bkf/pdb
• Related: 3BKT 3BKU
• Descriptor: Nickel-responsive regulator, ZINC ION (3 entities in total)
• Functional Keywords: nikr, nickel regulatory protein, transcription factor, beta sandwich, dna-binding, metal-binding, repressor, transcription regulation, metal binding protein
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 9855.66

Authors

Phillips, C.M.,Schreiter, E.R.,Drennan, C.L. (deposition date: 2007-12-06, release date: 2008-02-19, Last modification date: 2023-08-30)

Primary citation

Phillips, C.M.,Schreiter, E.R.,Guo, Y.,Wang, S.C.,Zamble, D.B.,Drennan, C.L.
Structural Basis of the Metal Specificity for Nickel Regulatory Protein NikR.
Biochemistry, 47:1938-1946, 2008

PubMed Abstract: In the presence of excess nickel, Escherichia coli NikR regulates cellular nickel uptake by suppressing the transcription of the nik operon, which encodes the nickel uptake transporter, NikABCDE. Previously published in vitro studies have shown that NikR is capable of binding a range of divalent transition metal ions in addition to Ni2+, including Co2+, Cu2+, Zn2+, and Cd2+. To understand how the high-affinity nickel binding site of NikR is able to accommodate these other metal ions, and to improve our understanding of NikR's mechanism of binding to DNA, we have determined structures of the metal-binding domain (MBD) of NikR in the apo form and in complex with Cu2+ and Zn2+ ions and compared them with the previously published structures with Ni2+. We observe that Cu2+ ions bind in a manner very similar to that of Ni2+, with a square planar geometry but with longer bond lengths. Crystals grown in the presence of Zn2+ reveal a protein structure similar to that of apo MBD with a disordered alpha3 helix, but with two electron density peaks near the Ni2+ binding site corresponding to two Zn2+ ions. These structural findings along with biochemical data on NikR support a hypothesis that ordering of the alpha3 helix is important for repressor activation.

PubMed: 18193897
DOI: 10.1021/bi702006h

Experimental method

X-RAY DIFFRACTION (1.9 Å)