ISDA: 4I8C

Deposition Date 2012-12-03

Release Date 2013-01-30

Last Version Date 2023-09-20

Entry Detail

PDB ID:

4I8C

Keywords:

TRANSPORT PROTEIN

Title:

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

Biological Source:

Source Organism(s):

Escherichia coli (Taxon ID: 83333)

Expression System(s):

Escherichia coli

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

2.50 Å

R-Value Free:

0.23

R-Value Work:

0.18

R-Value Observed:

0.19

Space Group:

P 62

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Macromolecular Entities

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:Nickel-binding periplasmic pr
Gene (Uniprot):nikA
Chain IDs:A, B, C
Chain Length:502
Number of Molecules:3
Biological Source:Escherichia coli

UniProt ID:P33590 Pfam ID:PF00496

Ligand Molecules

ACT

GOL

HIS

SO4

Primary Citation

The binding mode of Ni-((L)-His)(2) in NikA revealed by X-ray crystallography.

Lebrette, H, Iannello, M, Fontecilla-Camps, J.C, Cavazza, C.Show

J. Inorg. Biochem. 121C 16 18 (2012)

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

Abstact

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.

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Primary Citation of related structures

Abstact

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