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Literature summary for 5.6.1.7 extracted from

  • Cun, S.; Sun, H.
    A zinc-binding site by negative selection induces metallodrug susceptibility in an essential chaperonin (2010), Proc. Natl. Acad. Sci. USA, 107, 4943-4948.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.1.7

Protein Variants

Protein Variants Comment Organism
C51A wild-type HpGroES binds two Zn2+ per monomer. H45A, C51A, and C53A decrease to 0.3-0.5 Zn2+ per monomer Helicobacter pylori
C51A/C53A the double-cysteine mutant gives only 0.12 Zn2+ per monomer Helicobacter pylori
C53A wild-type HpGroES binds two Zn2+ per monomer. H45A, C51A, and C53A decrease to 0.3-0.5 Zn2+ per monomer Helicobacter pylori
H45A wild-type HpGroES binds two Zn2+ per monomer. H45A, C51A, and C53A decrease to 0.3-0.5 Zn2+ per monomer Helicobacter pylori
additional information wild-type HpGroES binds two Zn2+ per monomer, HpGroESDELTAMBD (MBD i.e. metalbinding domain) contains 0.71 per monomer Helicobacter pylori

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ His45, Cys51, and Cys53 make up an oxidation-sensitive zinc-binding site that may donate the bound metal to a zinc acceptor. Wild-type HpGroES binds two Zn2+ per monomer, HpGroESDELTAMBD (MBD i.e. metal-binding domain) contains 0.71 per monomer. H45A, C51A, and C53A decreased to 0.3-0.5 Zn2+ per monomer. The double-cysteine mutant (C51A/C53A) gives only 0.12 Zn2+ per monomer Helicobacter pylori

Organism

Organism UniProt Comment Textmining
Helicobacter pylori
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