4OES
Crystal structure of NikA from Brucella suis in complex with Fe(III)-EDTA
Summary for 4OES
| Entry DOI | 10.2210/pdb4oes/pdb |
| Related | 4OER |
| Descriptor | NikA protein, {[-(BIS-CARBOXYMETHYL-AMINO)-ETHYL]-CARBOXYMETHYL-AMINO}-ACETIC ACID, FE (III) ION, ... (6 entities in total) |
| Functional Keywords | extracytoplasmic, nickel import, metal transport, abc-type importer, extracytoplasmic nickel-binding protein, transport protein |
| Biological source | Brucella suis |
| Total number of polymer chains | 1 |
| Total formula weight | 56453.24 |
| Authors | Lebrette, H.,Cavazza, C. (deposition date: 2014-01-13, release date: 2014-10-01, Last modification date: 2023-09-20) |
| Primary citation | Lebrette, H.,Brochier-Armanet, C.,Zambelli, B.,de Reuse, H.,Borezee-Durant, E.,Ciurli, S.,Cavazza, C. Promiscuous nickel import in human pathogens: structure, thermodynamics, and evolution of extracytoplasmic nickel-binding proteins. Structure, 22:1421-1432, 2014 Cited by PubMed Abstract: 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. PubMed: 25199691DOI: 10.1016/j.str.2014.07.012 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.951 Å) |
Structure validation
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