5YH5

The crystal structure of Staphylococcus aureus CntA in apo form

Summary for 5YH5

• Entry DOI: 10.2210/pdb5yh5/pdb
• Descriptor: Nickel ABC transporter substrate-binding protein, 1,2-ETHANEDIOL, DI(HYDROXYETHYL)ETHER (3 entities in total)
• Functional Keywords: staphylococcus aureus, receptor, metal binding protein
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 1
• Total formula weight: 57824.15

Authors

Song, L.,Ji, Q. (deposition date: 2017-09-27, release date: 2018-03-28, Last modification date: 2024-03-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.9 Å)