3QIM

Histidine 416 of the periplamsic binding protein NikA is essential for nickel uptake in Escherichia coli

Summary for 3QIM

• Entry DOI: 10.2210/pdb3qim/pdb
• Descriptor: Nickel-binding periplasmic protein, GLYCEROL, ACETATE ION, ... (5 entities in total)
• Functional Keywords: metal transport, transport protein
• Biological source: Escherichia coli
• Cellular location: Periplasm (Probable): P33590
• Total number of polymer chains: 2
• Total formula weight: 114560.07

Authors

Cavazza, C.,Martin, L.,Laffly, E.,Lebrette, H.,Cherrier, M.V.,Zeppieri, L.,Richaud, P.,Carriere, M.,Fontecilla-Camps, J.C. (deposition date: 2011-01-27, release date: 2011-03-02, Last modification date: 2023-11-01)

Primary citation

Cavazza, C.,Martin, L.,Laffly, E.,Lebrette, H.,Cherrier, M.V.,Zeppieri, L.,Richaud, P.,Carriere, M.,Fontecilla-Camps, J.C.
Histidine 416 of the periplasmic binding protein NikA is essential for nickel uptake in Escherichia coli
Febs Lett., 585:711-715, 2011

PubMed Abstract: Escherichia coli require nickel for the synthesis of [NiFe] hydrogenases under anaerobic growth conditions. Nickel import depends on the specific ABC-transporter NikABCDE encoded by the nik operon, which deletion causes the complete abolition of hydrogenase activity. We have previously postulated that the periplasmic binding protein NikA binds a natural metallophore containing three carboxylate functions that coordinate a Ni(II) ion, the fourth ligand being His416, the only direct metal-protein contact, completing a square-planar coordination for the metal. The crystal structure of the H416I mutant showed no electron density corresponding to a metal-chelator complex. In vivo experiments indicate that the mutation causes a significant decrease in nickel uptake and hydrogenase activity. These results confirm the essential role of His416 in nickel transport by NikA.

PubMed: 21281641
DOI: 10.1016/j.febslet.2011.01.038

Experimental method

X-RAY DIFFRACTION (2.1 Å)