4OET

Crystal structure of NikZ from Campylobacter jejuni, unliganded form

4OET の概要

• エントリーDOI: 10.2210/pdb4oet/pdb
• 関連するPDBエントリー: 4OEU 4OEV
• 分子名称: Putative peptide ABC-transport system periplasmic peptide-binding protein, GLYCEROL (3 entities in total)
• 機能のキーワード: extracytoplasmic, nickel import, metal transport, abc-type importer, extracytoplasmic nickel-binding protein, transport protein
• 由来する生物種: Campylobacter jejuni
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 114367.60

構造登録者

Lebrette, H.,Cavazza, C. (登録日: 2014-01-13, 公開日: 2014-10-01, 最終更新日: 2023-09-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.4 Å)