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5YH8

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

Summary for 5YH8
Entry DOI10.2210/pdb5yh8/pdb
DescriptorNickel 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)
Functional Keywordscomplex, receptor, metal binding protein
Biological sourceStaphylococcus aureus
Total number of polymer chains1
Total formula weight59326.39
Authors
Ji, Q.,Song, L. (deposition date: 2017-09-27, release date: 2018-03-28, Last modification date: 2024-03-27)
Primary citationSong, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.12 Å)
Structure validation

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數據於2024-11-06公開中

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