ArticleProceedings of the National Academy of Sciences of the United States of America2010
A zinc-binding site by negative selection induces metallodrug susceptibility in an essential chaperonin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 48 citations in OpenAlex.
- Orally administered bismuth drug together withChemical science · 2022Article
- Metal Complexes as Antiviral Agents for SARS-CoV-2.Chembiochem : a European journal of chemical biology · 2021Review
- A novel mode of control of nickel uptake by a multifunctional metallochaperone.PLoS pathogens · 2021Article
- Metallodrug ranitidine bismuth citrate suppresses SARS-CoV-2 replication and relieves virus-associated pneumonia in Syrian hamsters.Nature microbiology · 2020Article
- Bismuth antimicrobial drugs serve as broad-spectrum metallo-β-lactamase inhibitors.Nature communications · 2018Article
- Identification of catabolite control protein A fromChemical science · 2017Article
- Functional disruption of peroxiredoxin by bismuth antiulcer drugs attenuates Helicobacter pylori survival.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Article
- Integrative approach for the analysis of the proteome-wide response to bismuth drugs inChemical science · 2017Article
- UreE-UreG complex facilitates nickel transfer and preactivates GTPase of UreG in Helicobacter pylori.The Journal of biological chemistry · 2015Article
- Current and potential applications of bismuth-based drugs.Molecules (Basel, Switzerland) · 2014Review
- Contributions of a disulfide bond and a reduced cysteine side chain to the intrinsic activity of the high-density lipoprotein receptor SR-BI.Biochemistry · 2012Article
- Recent advances in bioinorganic chemistry of bismuth.Current opinion in chemical biology · 2012Review
- Metallo-GTPase HypB from Helicobacter pylori and its interaction with nickel chaperone protein HypA.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
GroES is an indispensable chaperonin virtually found throughout all life forms. Consequently, mutations of this protein must be critically scrutinized by natural selection. Nevertheless, the homolog from a potentially virulent gastric pathogen, Helicobacter pylori, strikingly features a histidine/cysteine-rich C terminus that shares no significant homology with other family members. Additionally, three more (H45, C51, and C53) are uniquely present in its apical domain. The statistical analyses show that these residues may have originated from negative selection, presumably driven by either dependent or independent amino acid mutations. In the absence of the C-terminal metal-binding domain, the mutant protein still exhibits a substantial capacity for zinc binding in vivo. The biochemical properties of site-directed mutants indicate that H45, C51, and C53 make up an oxidation-sensitive zinc-binding site that may donate the bound metal to a zinc acceptor. Of interest, bismuth antiulcer drugs strongly bind at this site (K(d) of approximately 7 x 10(-26) M), replacing the bound zinc and consequently inducing the disruption of the quaternary structure. Because biological features by negative selection are usually inert to change during evolution, this study sheds light on a promising field whereby medicines can be designed or improved to specifically target the residues that uniquely evolved in pathogenic proteins so as to retard the emergence of drug resistance.
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