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Structure of the zinc transporter yiip

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.

Some assembly required: Constructing the elementary units of …

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 https://ltdesign-craft.com

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

Mechanism of Zinc Transport Through the Zinc Transporter YiiP - PMC

Category:Mechanism of Zinc Transport through the Zinc Transporter YiiP

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Structure of the zinc transporter yiip

RCSB PDB - 3J1Z: Inward-Facing Conformation of the Zinc Transporter …

WebStructural Basis for Auto-regulation of the Zinc Transporter YiiP - PMC Published in final edited form as: Escherichia coli mutant strain more tolerant to iron exposure 29, but whether YiiP is a bona fide ferrous iron efflux facilitator (FieF) remains controversial 14. Figure 2 … WebYiiP is a membrane transporter that catalyzes Zn2+/H+ exchange across the inner membrane of Escherichia coli. Mammalian homologs of YiiP play critical roles in zinc homeostasis and cell signaling. Here, we report the x-ray structure of YiiP in complex with zinc at 3.8 angstrom resolution.

Structure of the zinc transporter yiip

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WebFeb 28, 2024 · YiiP is a secondary transporter that couples Zn ²⁺ transport to the proton motive force. Structural studies of YiiP from prokaryotes as well as Znt8 from humans revealed three different Zn ² ... WebJun 27, 2007 · YiiP is a membrane transporter that catalyzes Zn2+/H+ exchange across the inner membrane of Escherichia coli. Mammalian homologs of YiiP play critical roles in …

WebBackground: YiiP is a bacterial zinc-for-proton antiporter belonging to the cation diffusion facilitator family. The zinc(II) ions are transported across the cell membrane, from the cytosol to the extracellular space. Methods: We performed atomistic molecular dynamics simulations of the YiiP dimer with zinc(II) ions in solution to elucidate how the metal ions … WebJul 24, 2012 · Inward-Facing Conformation of the Zinc Transporter YiiP revealed by Cryo-electron Microscopy. ... We used cryoelectron microscopy to determine a 13-Å resolution structure of a YiiP homolog from Shewanella oneidensis within a lipid bilayer in the absence of Zn(2+). Starting from the X-ray structure in the presence of Zn(2+), we used molecular ...

WebApr 29, 2009 · Structural basis for autoregulation of the zinc transporter YiiP. Zinc transporters have crucial roles in cellular zinc homeostatic control. The 2.9-A resolution … WebFeb 28, 2024 · This study enabled us to develop a hypothesis on the zinc efflux mechanism of YiiP. We have created six different models of YiiP representing the stages of the ion …

WebMar 5, 2024 · YiiP is a dimeric antiporter from the cation diffusion facilitator family that uses the proton motive force to transport Zn2+ across bacterial membranes. Previous work defined the atomic structure ... YiiP is a dimeric antiporter from the cation diffusion facilitator family that uses

WebThe crystal structure of YiiP revealed a tetrahedral transport site (binding site A; Figs. 2c and 3) with the compositionAsp45-Asp49–His153-Asp157(DD-HD),whereas the human orthologs, which are very specific for Zn2+, have an HD-HD binding site. laura hintonWebFeb 28, 2024 · The preference for the IF state even with the presence of the Zn 2+ ion maybe be the result of the unique helical crystalline structure adopted by soYiiP and used in the EM studies. 10 The I Z complex is a Zn 2+ loaded YiiP embedded in a DOPC bilayer, comprised of eight zinc ions located at all three zinc-binding sites (i.e., ZnA, ZnB, and ZnC). aukera bloisWebNov 12, 2024 · Given that we have previously shown that the ZnT2 model, which is also based on YiiP, is able to predict the zinc permeation pathway along the transporter 29, and given the very low homology ... laura hittinger