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Metal Binding Properties of Escherichia coli YjiA, a Member of the Metal Homeostasis-Associated COG0523 Family of GTPases

[Image: see text] GTPases are critical molecular switches involved in a wide range of biological functions. Recent phylogenetic and genomic analyses of the large, mostly uncharacterized COG0523 subfamily of GTPases revealed a link between some COG0523 proteins and metal homeostasis pathways. In this...

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Autores principales: Sydor, Andrew M., Jost, Marco, Ryan, Katherine S., Turo, Kaitlyn E., Douglas, Colin D., Drennan, Catherine L., Zamble, Deborah B.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2013
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3596956/
https://www.ncbi.nlm.nih.gov/pubmed/24449932
http://dx.doi.org/10.1021/bi301600z
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author Sydor, Andrew M.
Jost, Marco
Ryan, Katherine S.
Turo, Kaitlyn E.
Douglas, Colin D.
Drennan, Catherine L.
Zamble, Deborah B.
author_facet Sydor, Andrew M.
Jost, Marco
Ryan, Katherine S.
Turo, Kaitlyn E.
Douglas, Colin D.
Drennan, Catherine L.
Zamble, Deborah B.
author_sort Sydor, Andrew M.
collection PubMed
description [Image: see text] GTPases are critical molecular switches involved in a wide range of biological functions. Recent phylogenetic and genomic analyses of the large, mostly uncharacterized COG0523 subfamily of GTPases revealed a link between some COG0523 proteins and metal homeostasis pathways. In this report, we detail the bioinorganic characterization of YjiA, a representative member of COG0523 subgroup 9 and the only COG0523 protein to date with high-resolution structural information. We find that YjiA is capable of binding several types of transition metals with dissociation constants in the low micromolar range and that metal binding affects both the oligomeric structure and GTPase activity of the enzyme. Using a combination of X-ray crystallography and site-directed mutagenesis, we identify, among others, a metal-binding site adjacent to the nucleotide-binding site in the GTPase domain that involves a conserved cysteine and several glutamate residues. Mutations of the coordinating residues decrease the impact of metal, suggesting that metal binding to this site is responsible for modulating the GTPase activity of the protein. These findings point toward a regulatory function for these COG0523 GTPases that is responsive to their metal-bound state.
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spelling pubmed-35969562013-03-14 Metal Binding Properties of Escherichia coli YjiA, a Member of the Metal Homeostasis-Associated COG0523 Family of GTPases Sydor, Andrew M. Jost, Marco Ryan, Katherine S. Turo, Kaitlyn E. Douglas, Colin D. Drennan, Catherine L. Zamble, Deborah B. Biochemistry [Image: see text] GTPases are critical molecular switches involved in a wide range of biological functions. Recent phylogenetic and genomic analyses of the large, mostly uncharacterized COG0523 subfamily of GTPases revealed a link between some COG0523 proteins and metal homeostasis pathways. In this report, we detail the bioinorganic characterization of YjiA, a representative member of COG0523 subgroup 9 and the only COG0523 protein to date with high-resolution structural information. We find that YjiA is capable of binding several types of transition metals with dissociation constants in the low micromolar range and that metal binding affects both the oligomeric structure and GTPase activity of the enzyme. Using a combination of X-ray crystallography and site-directed mutagenesis, we identify, among others, a metal-binding site adjacent to the nucleotide-binding site in the GTPase domain that involves a conserved cysteine and several glutamate residues. Mutations of the coordinating residues decrease the impact of metal, suggesting that metal binding to this site is responsible for modulating the GTPase activity of the protein. These findings point toward a regulatory function for these COG0523 GTPases that is responsive to their metal-bound state. American Chemical Society 2013-02-13 2013-03-12 /pmc/articles/PMC3596956/ /pubmed/24449932 http://dx.doi.org/10.1021/bi301600z Text en Copyright © 2013 American Chemical Society
spellingShingle Sydor, Andrew M.
Jost, Marco
Ryan, Katherine S.
Turo, Kaitlyn E.
Douglas, Colin D.
Drennan, Catherine L.
Zamble, Deborah B.
Metal Binding Properties of Escherichia coli YjiA, a Member of the Metal Homeostasis-Associated COG0523 Family of GTPases
title Metal Binding Properties of Escherichia coli YjiA, a Member of the Metal Homeostasis-Associated COG0523 Family of GTPases
title_full Metal Binding Properties of Escherichia coli YjiA, a Member of the Metal Homeostasis-Associated COG0523 Family of GTPases
title_fullStr Metal Binding Properties of Escherichia coli YjiA, a Member of the Metal Homeostasis-Associated COG0523 Family of GTPases
title_full_unstemmed Metal Binding Properties of Escherichia coli YjiA, a Member of the Metal Homeostasis-Associated COG0523 Family of GTPases
title_short Metal Binding Properties of Escherichia coli YjiA, a Member of the Metal Homeostasis-Associated COG0523 Family of GTPases
title_sort metal binding properties of escherichia coli yjia, a member of the metal homeostasis-associated cog0523 family of gtpases
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3596956/
https://www.ncbi.nlm.nih.gov/pubmed/24449932
http://dx.doi.org/10.1021/bi301600z
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