4I8C: X-ray Structure of Nika in Complex With Ni-(l-his)2

Citation:
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.
PDB ID: 4I8CDownload
MMDB ID: 107202
PDB Deposition Date: 2012/12/3
Updated in MMDB: 2013/02
Experimental Method:
x-ray diffraction
Resolution: 2.5  Å
Source Organism:
Similar Structures:
Biological Unit for 4I8C: monomeric; determined by author and by software (PISA)
Molecular Components in 4I8C
Label Count Molecule
Protein (1 molecule)
1
Nickel-binding Periplasmic Protein
Molecule annotation
Chemicals (14 molecules)
1
2
2
1
3
7
4
4
* Click molecule labels to explore molecular sequence information.

Citing MMDB
.