Journal article
A trap-door mechanism for zinc acquisition by streptococcus pneumoniae adca
Z Luo, JR Morey, E Deplazes, A Motygullina, A Tan, K Ganio, SL Neville, N Eleftheriadis, M Isselstein, VG Pederick, JC Paton, T Cordes, JR Harmer, B Kobe, CA McDevitt
Mbio | AMER SOC MICROBIOLOGY | Published : 2021
Abstract
Zinc is an essential element in all domains of life. Nonetheless, how pro-karyotes achieve selective acquisition of zinc from the extracellular environment remains poorly understood. Here, we elucidate a novel mechanism for zinc-binding in AdcA, a solute-binding protein of Streptococcus pneumoniae. Crystal structure analyses reveal the two-domain organization of the protein and show that only the N-terminal domain (AdcAN) is necessary for zinc import. Zinc binding induces only minor changes in the global protein conformation of AdcA and stabilizes a highly mobile loop within the AdcAN domain. This loop region, which is conserved in zinc-specific solute-binding proteins, facilitates closure o..
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Grants
Awarded by Australian Research Council