3qim

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

spinqualitylabelsall models 3qim, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3qim is a 2 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: ACT, GOL, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NIKA_ECOLI Involved in a nickel transport system, probably represents the nickel binder. Publication Abstract from PubMed 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. Histidine 416 of the periplasmic binding protein NikA is essential for nickel uptake in Escherichia coli.,Cavazza C, Martin L, Laffly E, Lebrette H, Cherrier MV, Zeppieri L, Richaud P, Carriere M, Fontecilla-Camps JC FEBS Lett. 2011 Feb 18;585(4):711-5. Epub 2011 Feb 1. PMID:21281641 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ABC transporter 3D structures

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