4OFL

Crystal structure of YntA from Yersinia pestis in complex with Ni(L-His)2

Summary for 4OFL

• Entry DOI: 10.2210/pdb4ofl/pdb
• Related: 4OFO
• Descriptor: Extracytoplasmic Nickel-Binding Protein YpYntA, NICKEL (II) ION, HISTIDINE, ... (4 entities in total)
• Functional Keywords: nickel import, periplasmic, abc-type importer, extracytoplasmic nickel-binding protein, transport protein
• Biological source: Yersinia pestis
• Total number of polymer chains: 2
• Total formula weight: 110749.13

Authors

Lebrette, H.,Cavazza, C. (deposition date: 2014-01-15, release date: 2014-10-01, Last modification date: 2024-10-16)

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

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: 25199691
DOI: 10.1016/j.str.2014.07.012

Experimental method

X-RAY DIFFRACTION (2.7 Å)