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The crystal structure of Staphylococcus aureus CntA in complex with staphylopine and nickelThe crystal structure of Staphylococcus aureus CntA in complex with staphylopine and nickel
Structural highlights
Publication Abstract from PubMedMetal acquisition is vital to pathogens for successful infection within hosts. Staphylopine (StP), a broad-spectrum metallophore biosynthesized by the major human pathogen, Staphylococcus aureus, 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. Mechanistic insights into staphylopine-mediated metal acquisition.,Song L, Zhang Y, Chen W, Gu T, Zhang SY, Ji Q Proc Natl Acad Sci U S A. 2018 Mar 26. pii: 1718382115. doi:, 10.1073/pnas.1718382115. PMID:29581261[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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