4I8C

X-ray structure of NikA in complex with Ni-(L-His)2

Summary for 4I8C

• Entry DOI: 10.2210/pdb4i8c/pdb
• Descriptor: Nickel-binding periplasmic protein, HISTIDINE, NICKEL (II) ION, ... (8 entities in total)
• Functional Keywords: transport protein
• Biological source: Escherichia coli
• Total number of polymer chains: 3
• Total formula weight: 172104.29

Authors

Lebrette, H.,Iannello, M.,Fontecilla-Camps, J.C.,Cavazza, C. (deposition date: 2012-12-03, release date: 2013-01-30, Last modification date: 2023-09-20)

Primary citation

Lebrette, H.,Iannello, M.,Fontecilla-Camps, J.C.,Cavazza, C.
The binding mode of Ni-((L)-His)(2) in NikA revealed by X-ray crystallography.
J.Inorg.Biochem., 121C:16-18, 2012

PubMed Abstract: The ABC-type importer NikABCDE mediates nickel acquisition in Escherichia coli. The periplasmic nickel-binding component NikA has a folding similar to that of the peptide transporter OppA and does not bind free nickel. Instead, we showed that the metal is tetra-coordinated by an organic tri-dentate molecule and His416. Conversely, it has been recently reported that NikA binds Ni-(L-His)2 and that addition of histidine increases the rate of nickel uptake in vivo. Here, we report the structure of NikA/Ni-(L-His)2 and show that histidine binding differs from peptide binding in OppA. The structure also confirms the central role of His416 in nickel binding.

PubMed: 23314594
DOI: 10.1016/j.jinorgbio.2012.12.010

Experimental method

X-RAY DIFFRACTION (2.503 Å)