ArticleBiochemistry2013
Metal binding properties of Escherichia coli YjiA, a member of the metal homeostasis-associated COG0523 family of GTPases.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 55 citations in OpenAlex.
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- "Self-gapping" by a C-terminal domain arginine finger regulates GTP hydrolysis in bacterial zinc metallochaperones.bioRxiv : the preprint server for biology · 2026Article
- Zinc-metallochaperones ofMicrobiology spectrum · 2025Article
- Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking.Chemical reviews · 2024Review
- Structure of a dimeric full-length ABC transporter.Nature communications · 2024Article
- The metal-binding GTPases CobW2 and CobW3 are at the crossroads of zinc and cobalt homeostasis inJournal of bacteriology · 2024Article
- Coupling of zinc and GTP binding drives G-domain folding in Acinetobacter baumannii ZigA.Biophysical journal · 2024Article
- A critical role for iron and zinc homeostatic systems in the evolutionary adaptation ofMicrobial genomics · 2023Article
- Moving metals: How microbes deliver metal cofactors to metalloproteins.Molecular microbiology · 2023Article
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- The role of nucleoside triphosphate hydrolase metallochaperones in making metalloenzymes.Metallomics : integrated biometal science · 2022Review
- Adaptive responses of marine diatoms to zinc scarcity and ecological implications.Nature communications · 2022Article
- Genome-wide identification and characterization of Fur-binding sites in the cyanobacteria Synechocystis sp. PCC 6803 and PCC 6714.DNA research : an international journal for rapid publication of reports on genes and genomes · 2021Article
- COG0523 proteins: a functionally diverse family of transition metal-regulated G3E P-loop GTP hydrolases from bacteria to man.Metallomics : integrated biometal science · 2021Article
- Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.Chemical reviews · 2021Review
- Zur: Zinc-Sensing Transcriptional Regulator in a Diverse Set of Bacterial Species.Pathogens (Basel, Switzerland) · 2021Review
- Shulin packages axonemal outer dynein arms for ciliary targeting.Science (New York, N.Y.) · 2021Article
- Calculating metalation in cells reveals CobW acquires CoNature communications · 2021Article
Corrections and comments
- Erratum issued
Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
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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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.