Two zinc-binding domains in the transporter AdcA from Streptococcus pyogenes facilitate high-affinity binding and fast transport of zinc

The Journal of Biological Chemistry
Kun CaoXuesong Sun

Abstract

Zinc is an essential metal in bacteria. One important bacterial zinc transporter is AdcA, and most bacteria possess AdcA homologs that are single-domain small proteins due to better efficiency of protein biogenesis. However, a double-domain AdcA with two zinc-binding sites is significantly overrepresented in Streptococcus species, many of which are major human pathogens. Using molecular simulation and experimental validations of AdcA from Streptococcus pyogenes, we found here that the two AdcA domains sequentially stabilize the structure upon zinc binding, indicating an organization required for both increased zinc affinity and transfer speed. This structural organization appears to endow Streptococcus species with distinct advantages in zinc-depleted environments, which would not be achieved by each single AdcA domain alone. This enhanced zinc transport mechanism sheds light on the significance of the evolution of the AdcA domain fusion, provides new insights into double-domain transporter proteins with two binding sites for the same ion, and indicates a potential target of antimicrobial drugs against pathogenic Streptococcus species.

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Citations

Aug 21, 2019·Communications Biology·Durga Prasad NeupaneErik Thomas Yukl
Oct 7, 2020·Computational and Structural Biotechnology Journal·Panupong MahalapbutrThanyada Rungrotmongkol
Feb 2, 2021·Journal of Molecular Liquids·Tuanjai SomboonThanyada Rungrotmongkol
Feb 4, 2021·MBio·Zhenyao LuoChristopher A McDevitt
Jan 12, 2021·Frontiers in Microbiology·Cinthia Alves-BarrocoAlexandra R Fernandes
Nov 19, 2019·Current Topics in Medicinal Chemistry·Panupong MahalapbutrThanyada Rungrotmongkol
Jan 12, 2020·Communications Biology·Durga Prasad NeupaneErik Thomas Yukl

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