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Structural Basis for Auto-regulation of the Zinc Transporter YiiP
Zinc transporters play critical roles in cellular zinc homeostatic control. The 2.9-Å resolution structure of the zinc transporter YiiP from Escherichia coli reveals a richly charged dimer-interface stabilized by zinc binding. Site-directed fluorescent resonance energy transfer (FRET) measurements a...
Autores principales: | , , |
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Formato: | Texto |
Lenguaje: | English |
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2009
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2758918/ https://www.ncbi.nlm.nih.gov/pubmed/19749753 http://dx.doi.org/10.1038/nsmb.1662 |
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author | Lu, Min Chai, Jin Fu, Dax |
author_facet | Lu, Min Chai, Jin Fu, Dax |
author_sort | Lu, Min |
collection | PubMed |
description | Zinc transporters play critical roles in cellular zinc homeostatic control. The 2.9-Å resolution structure of the zinc transporter YiiP from Escherichia coli reveals a richly charged dimer-interface stabilized by zinc binding. Site-directed fluorescent resonance energy transfer (FRET) measurements and mutation-activity analysis suggest that zinc binding triggers hinge movements of two electrically repulsive cytoplasmic domains pivoting around four salt-bridges situated at the juncture of the cytoplasmic and transmembrane domains. These highly conserved salt-bridges interlock transmembrane helices at the dimer-interface, well positioned to transmit zinc-induced inter-domain movements to reorient transmembrane helices, thereby modulating coordination geometry of the active-site for zinc transport. The cytoplasmic domain of YiiP is a structural mimic of metal trafficking proteins and the metal-binding domains of metal-transporting P-type ATPases. The use of this common structural module to regulate metal coordination chemistry may enable a tunable transport activity in response to cytoplasmic metal fluctuations. |
format | Text |
id | pubmed-2758918 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
record_format | MEDLINE/PubMed |
spelling | pubmed-27589182010-04-01 Structural Basis for Auto-regulation of the Zinc Transporter YiiP Lu, Min Chai, Jin Fu, Dax Nat Struct Mol Biol Article Zinc transporters play critical roles in cellular zinc homeostatic control. The 2.9-Å resolution structure of the zinc transporter YiiP from Escherichia coli reveals a richly charged dimer-interface stabilized by zinc binding. Site-directed fluorescent resonance energy transfer (FRET) measurements and mutation-activity analysis suggest that zinc binding triggers hinge movements of two electrically repulsive cytoplasmic domains pivoting around four salt-bridges situated at the juncture of the cytoplasmic and transmembrane domains. These highly conserved salt-bridges interlock transmembrane helices at the dimer-interface, well positioned to transmit zinc-induced inter-domain movements to reorient transmembrane helices, thereby modulating coordination geometry of the active-site for zinc transport. The cytoplasmic domain of YiiP is a structural mimic of metal trafficking proteins and the metal-binding domains of metal-transporting P-type ATPases. The use of this common structural module to regulate metal coordination chemistry may enable a tunable transport activity in response to cytoplasmic metal fluctuations. 2009-09-13 2009-10 /pmc/articles/PMC2758918/ /pubmed/19749753 http://dx.doi.org/10.1038/nsmb.1662 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms |
spellingShingle | Article Lu, Min Chai, Jin Fu, Dax Structural Basis for Auto-regulation of the Zinc Transporter YiiP |
title | Structural Basis for Auto-regulation of the Zinc Transporter YiiP |
title_full | Structural Basis for Auto-regulation of the Zinc Transporter YiiP |
title_fullStr | Structural Basis for Auto-regulation of the Zinc Transporter YiiP |
title_full_unstemmed | Structural Basis for Auto-regulation of the Zinc Transporter YiiP |
title_short | Structural Basis for Auto-regulation of the Zinc Transporter YiiP |
title_sort | structural basis for auto-regulation of the zinc transporter yiip |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2758918/ https://www.ncbi.nlm.nih.gov/pubmed/19749753 http://dx.doi.org/10.1038/nsmb.1662 |
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