Pneumococcal histidine triads – involved not only in Zn2+, but also Ni2+ binding?
| Autor: | Hanna Czapor-Irzabek, Adriana Miller, Henryk Kozlowski, Dorota Dudek, Magdalena Rowińska-Żyrek, Slawomir Potocki |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
inorganic chemicals
0301 basic medicine Chemistry 030106 microbiology Significant difference Metals and Alloys Biophysics Virulence Bioinorganic chemistry medicine.disease_cause Biochemistry Biomaterials 03 medical and health sciences Chemistry (miscellaneous) Streptococcus pneumoniae medicine Binding site Histidine |
| Zdroj: | Metallomics. 10(11):1631-1637 |
| ISSN: | 1756-5901 |
| Popis: | Polyhistidine triad proteins, which participate in Zn2+ uptake in Streptococcus pneumoniae, contain multiple copies of the HxxHxH (histidine triad motif) sequence. We focus on three such motifs from one of the most common and well-conserved polyhistidine triad proteins, PhtA, in order to understand their bioinorganic chemistry; particular focus is given to (i) understanding which of the PhtA triads binds Zn2+ with the highest affinity (and why) and (ii) explaining whether Ni2+ (also crucial for bacterial survival and virulence) could potentially outcompete Zn2+ at its native binding site. There is no significant difference in the stability of zinc(II) complexes with the three studied protein fragments, but one of the nickel(II)–polyhistidine triads is remarkably stable; we explain why and hypothesize about the biological importance of this finding. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|