4oev

Crystal structure of NikZ from Campylobacter jejuni in complex with Ni(II) ion

spinqualitylabelsall models 4oev, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4oev is a 2 chain structure with sequence from Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: GOL, NI, OXL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q0P844_CAMJE Publication Abstract from PubMed In human pathogenic bacteria, nickel is required for the activation of two enzymes, urease and [NiFe]-hydrogenase, necessary for host infection. Acquisition of Ni(II) is mediated by either permeases or ABC-importers, the latter including a subclass that involves an extracytoplasmic nickel-binding protein, Ni-BP. This study reports on the structure of three Ni-BPs from a diversity of human pathogens and on the existence of three new nickel-binding motifs. These are different from that previously described for Escherichia coli Ni-BP NikA, known to bind nickel via a nickelophore, and indicate a variegated ligand selectivity for Ni-BPs. The structures are consistent with ligand affinities measured in solution by calorimetry and challenge the hypothesis of a general requirement of nickelophores for nickel uptake by canonical ABC importers. Phylogenetic analyses showed that Ni-BPs have different evolutionary origins and emerged independently from peptide-binding proteins, possibly explaining the promiscuous behavior of this class of Ni(II) carriers. Promiscuous Nickel Import in Human Pathogens: Structure, Thermodynamics, and Evolution of Extracytoplasmic Nickel-Binding Proteins.,Lebrette H, Brochier-Armanet C, Zambelli B, de Reuse H, Borezee-Durant E, Ciurli S, Cavazza C Structure. 2014 Sep 3. pii: S0969-2126(14)00243-3. doi:, 10.1016/j.str.2014.07.012. PMID:25199691 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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