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RESEARCH PRODUCT
Pneumococcal HxxHxH triad – Copper(II) interactions – How important is the ‘x’?
Dorota DudekAnna JanickaSlawomir PotockiPaula DelgadoMagdalena Rowinska-zyrekHenryk KozłowskiHenryk Kozlowskisubject
biology010405 organic chemistryChemistryStereochemistryVirulencechemistry.chemical_elementBioinorganic chemistry010402 general chemistrymedicine.disease_causebiology.organism_classification01 natural sciencesDNA-binding proteinCopper0104 chemical sciencesInorganic ChemistryMetalvisual_artStreptococcus pneumoniaeMaterials Chemistrymedicinevisual_art.visual_art_mediumPhysical and Theoretical ChemistryBinding siteBacteriadescription
Abstract PhtA, a Streptococcus pneumoniae polyhistidine triad protein, which contributes to virulence by interacting with components of the immune system, by being involved in adherence of bacteria and in Zn(II) uptake, contains five copies of the HxxHxH sequence. Since this motif is also present in numerous Cu(II) binding proteins, we decided to focus on the bioinorganic chemistry of copper(II) with three of such PhtA repeats, in order to understand which of the PhtA triads binds Cu(II) with the highest affinity and explain if Cu(II) would be able to outcompete Zn(II) from its native binding site under physiological metal concentrations.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2019-03-01 | Inorganica Chimica Acta |