WebFeb 23, 2024 · YiiP is a prokaryotic Zn 2+ /H + antiporter that serves as a model for the Cation Diffusion Facilitator (CDF) superfamily, members of which are generally … WebUnbalanced levels of zinc in cells can result in various pathological conditions. In the current work, all-atom molecular dynamics simulations were used to study the structure-function correlation between different YiiP states embedded in a lipid bilayer. This study enabled us to develop a hypothesis on the zinc efflux mechanism of YiiP.
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WebMechanism of Zinc Transport through the Zinc Transporter YiiP J Chem Theory Comput. 2024 Feb 28. doi: 10.1021/acs.jctc.1c00927. Online ahead of print. Authors Gaurav … WebMar 1, 2024 · Zinc transporter 8 (ZnT8) is mainly expressed in pancreatic islet β cells and is responsible for H +-coupled uptake (antiport) of Zn 2+ into the lumen of insulin secretory granules. Structures of human ZnT8 and its prokaryotic homolog YiiP have provided structural basis for constructing a plausible transport cycle for Zn 2+.However, the … auken
Structure of The Zinc Transporter YiiP (Journal Article) OSTI.GOV
WebStructural basis for autoregulation of the zinc transporter YiiP Min Lu, Jin Chai & Dax Fu from Escherichia coli reveals a richly charged dimer interface stabilized by zinc binding. Web1 day ago · Abstract. YiiP is a prokaryotic Zn 2+ /H + antiporter that serves as a model for the Cation Diffusion Facilitator (CDF) superfamily, members of which are generally … WebApr 12, 2024 · We report the structure of the Pseudomonas aeruginosa nocardamine transporter FoxA bound to the xenosiderophore, bisucaberin. The interactions revealed by this co-structure help to explain how the thiopeptide antibiotic thiocillin may bind FoxA. Distinct residues are important for recognition, uptake, and signaling by the three ligands. aukey 2 in 1