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3DP8

Structural characterization of a putative endogenous metal chelator in the periplasmic nickel transporter NikA (nickel butane-1,2,4-tricarboxylate form)

Summary for 3DP8
Entry DOI10.2210/pdb3dp8/pdb
Related1UIU 1UIV 1ZLQ 2NOO
DescriptorNickel-binding periplasmic protein, NICKEL (II) ION, ACETATE ION, ... (8 entities in total)
Functional Keywordsnickel, nickellophore, butane-1, 2, 4-tricarboxylate, transport, metal transport
Biological sourceEscherichia coli
Cellular locationPeriplasm (Probable): P33590
Total number of polymer chains3
Total formula weight171559.20
Authors
Cherrier, M.V.,Cavazza, C.,Bochot, C.,Lemaire, D.,Fontecilla-Camps, J.C. (deposition date: 2008-07-07, release date: 2008-09-16, Last modification date: 2023-11-01)
Primary citationCherrier, M.V.,Cavazza, C.,Bochot, C.,Lemaire, D.,Fontecilla-Camps, J.C.
Structural characterization of a putative endogenous metal chelator in the periplasmic nickel transporter NikA
Biochemistry, 47:9937-9943, 2008
Cited by
PubMed Abstract: Escherichia coli and related bacteria require nickel for the synthesis of hydrogenases, enzymes involved in hydrogen oxidation and proton reduction. Nickel transport to the cytoplasm depends on five proteins, NikA-E. We have previously reported the three-dimensional structure of the soluble periplasmic nickel transporter NikA in a complex with FeEDTA(H 2O) (-). We have now determined the structure of EDTA-free NikA and have found that it binds a small organic molecule that contributes three ligands to the coordination of a transition metal ion. Unexpectedly, His416, which was far from the metal-binding site in the FeEDTA(H 2O) (-)-NikA complex, becomes the fourth observed ligand to the metal. The best match to the omit map electron density is obtained for butane-1,2,4-tricarboxylate (BTC). Our attempts to obtain a BTC-Ni-NikA complex using apo protein and commercial reagents resulted in nickel-free BTC-NikA. Overall, our results suggest that nickel transport in vivo requires a specific metallophore that may be BTC.
PubMed: 18759453
DOI: 10.1021/bi801051y
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

237735

數據於2025-06-18公開中

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