5YH8

The crystal structure of Staphylococcus aureus CntA in complex with staphylopine and nickel

5YH8 の概要

• エントリーDOI: 10.2210/pdb5yh8/pdb
• 分子名称: Nickel ABC transporter substrate-binding protein, NICKEL (II) ION, (2~{S})-4-[[(2~{R})-3-(1~{H}-imidazol-4-yl)-1-oxidanyl-1-oxidanylidene-propan-2-yl]amino]-2-[[(2~{S})-1-oxidanyl-1-oxidanylidene-propan-2-yl]amino]butanoic acid, ... (6 entities in total)
• 機能のキーワード: complex, receptor, metal binding protein
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 59326.39

構造登録者

Ji, Q.,Song, L. (登録日: 2017-09-27, 公開日: 2018-03-28, 最終更新日: 2024-03-27)

主引用文献

Song, L.,Zhang, Y.,Chen, W.,Gu, T.,Zhang, S.Y.,Ji, Q.
Mechanistic insights into staphylopine-mediated metal acquisition
Proc. Natl. Acad. Sci. U.S.A., 115:3942-3947, 2018

PubMed Abstract: Metal acquisition is vital to pathogens for successful infection within hosts. Staphylopine (StP), a broad-spectrum metallophore biosynthesized by the major human pathogen, , plays a central role in transition-metal acquisition and bacterial virulence. The StP-like biosynthesis loci are present in various pathogens, and the proteins responsible for StP/metal transportation have been determined. However, the molecular mechanisms of how StP/metal complexes are recognized and transported remain unknown. We report multiple structures of the extracytoplasmic solute-binding protein CntA from the StP/metal transportation system in apo form and in complex with StP and three different metals. We elucidated a sophisticated metal-bound StP recognition mechanism and determined that StP/metal binding triggers a notable interdomain conformational change in CntA. Furthermore, CRISPR/Cas9-mediated single-base substitution mutations and biochemical analysis highlight the importance of StP/metal recognition for StP/metal acquisition. These discoveries provide critical insights into the study of novel metal-acquisition mechanisms in microbes.

PubMed: 29581261
DOI: 10.1073/pnas.1718382115

実験手法

X-RAY DIFFRACTION (2.12 Å)