1. The binding mode of Ni-(L-His)2 in NikA revealed by X-ray crystallography
- Author
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Christine Cavazza, Marina Iannello, Juan C. Fontecilla-Camps, Hugo Lebrette, Institut de biologie structurale (IBS - UMR 5075 ), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Cristallographie et Cristallogénèse des Protéines (LCCP), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)
- Subjects
inorganic chemicals ,Protein Folding ,MESH: Protein Folding ,Lipoproteins ,chemistry.chemical_element ,Peptide ,Peptide binding ,MESH: Carrier Proteins ,MESH: Escherichia coli Proteins ,Plasma protein binding ,010402 general chemistry ,Crystallography, X-Ray ,01 natural sciences ,Biochemistry ,Inorganic Chemistry ,03 medical and health sciences ,MESH: Histidine ,MESH: Coordination Complexes ,Coordination Complexes ,Nickel ,MESH: Nickel ,otorhinolaryngologic diseases ,Escherichia coli ,MESH: Protein Binding ,Histidine ,Binding site ,030304 developmental biology ,chemistry.chemical_classification ,0303 health sciences ,Binding Sites ,[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM] ,Chemistry ,MESH: Escherichia coli ,Escherichia coli Proteins ,MESH: Models, Chemical ,Periplasmic space ,MESH: Crystallography, X-Ray ,MESH: Lipoproteins ,0104 chemical sciences ,Crystallography ,MESH: Binding Sites ,Models, Chemical ,MESH: ATP-Binding Cassette Transporters ,Protein folding ,ATP-Binding Cassette Transporters ,Carrier Proteins ,Protein Binding - Abstract
International audience; 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.
- Published
- 2012
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