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Conformational flexibility in the zinc solute-binding protein ZnuA

Zinc is an essential metal for all kingdoms of life, making its transport across the cell membrane a critical function. In bacteria, high-affinity zinc import is accomplished by ATP-binding cassette (ABC) transporters, which rely on extracellular solute-binding proteins (SBPs) of cluster A-I to acqu...

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Autores principales: Yekwa, Elsie Laban, Serrano, Fred Allen, Yukl, Erik
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8900738/
https://www.ncbi.nlm.nih.gov/pubmed/35234138
http://dx.doi.org/10.1107/S2053230X22001662
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author Yekwa, Elsie Laban
Serrano, Fred Allen
Yukl, Erik
author_facet Yekwa, Elsie Laban
Serrano, Fred Allen
Yukl, Erik
author_sort Yekwa, Elsie Laban
collection PubMed
description Zinc is an essential metal for all kingdoms of life, making its transport across the cell membrane a critical function. In bacteria, high-affinity zinc import is accomplished by ATP-binding cassette (ABC) transporters, which rely on extracellular solute-binding proteins (SBPs) of cluster A-I to acquire the metal and deliver it to the membrane permease. These systems are important for survival and virulence, making them attractive targets for the development of novel antibiotics. Citrobacter koseri is an emerging pathogen with extensive antibiotic resistance. High-affinity zinc binding to the C. koseri cluster A-I SBP ZnuA has been characterized and the structure of the zinc-bound (holo) form has been determined by X-ray crystallography. Remarkably, despite 95% sequence identity to the ZnuA homologue from Salmonella enterica, C. koseri ZnuA exhibits a different zinc-coordination environment and a closed rather than an open conformation. Comparison with structures of another close ZnuA homologue from Escherichia coli suggests a surprisingly flexible conformational landscape that may be important for efficient zinc binding and/or delivery to the membrane permease.
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spelling pubmed-89007382022-03-29 Conformational flexibility in the zinc solute-binding protein ZnuA Yekwa, Elsie Laban Serrano, Fred Allen Yukl, Erik Acta Crystallogr F Struct Biol Commun Research Communications Zinc is an essential metal for all kingdoms of life, making its transport across the cell membrane a critical function. In bacteria, high-affinity zinc import is accomplished by ATP-binding cassette (ABC) transporters, which rely on extracellular solute-binding proteins (SBPs) of cluster A-I to acquire the metal and deliver it to the membrane permease. These systems are important for survival and virulence, making them attractive targets for the development of novel antibiotics. Citrobacter koseri is an emerging pathogen with extensive antibiotic resistance. High-affinity zinc binding to the C. koseri cluster A-I SBP ZnuA has been characterized and the structure of the zinc-bound (holo) form has been determined by X-ray crystallography. Remarkably, despite 95% sequence identity to the ZnuA homologue from Salmonella enterica, C. koseri ZnuA exhibits a different zinc-coordination environment and a closed rather than an open conformation. Comparison with structures of another close ZnuA homologue from Escherichia coli suggests a surprisingly flexible conformational landscape that may be important for efficient zinc binding and/or delivery to the membrane permease. International Union of Crystallography 2022-02-28 /pmc/articles/PMC8900738/ /pubmed/35234138 http://dx.doi.org/10.1107/S2053230X22001662 Text en © Yekwa, Serrano & Yukl 2022 https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
spellingShingle Research Communications
Yekwa, Elsie Laban
Serrano, Fred Allen
Yukl, Erik
Conformational flexibility in the zinc solute-binding protein ZnuA
title Conformational flexibility in the zinc solute-binding protein ZnuA
title_full Conformational flexibility in the zinc solute-binding protein ZnuA
title_fullStr Conformational flexibility in the zinc solute-binding protein ZnuA
title_full_unstemmed Conformational flexibility in the zinc solute-binding protein ZnuA
title_short Conformational flexibility in the zinc solute-binding protein ZnuA
title_sort conformational flexibility in the zinc solute-binding protein znua
topic Research Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8900738/
https://www.ncbi.nlm.nih.gov/pubmed/35234138
http://dx.doi.org/10.1107/S2053230X22001662
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