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  • Title: Structural characterisation of the HT3 motif of the polyhistidine triad protein D from Streptococcus pneumoniae.
    Author: Luo Z, Pederick VG, Paton JC, McDevitt CA, Kobe B.
    Journal: FEBS Lett; 2018 Jul; 592(13):2341-2350. PubMed ID: 29856892.
    Abstract:
    The bacterium Streptococcus pneumoniae (the pneumococcus) is a major human pathogen that requires Zn2+ for its survival and virulence in the host environment. Polyhistidine triad protein D (PhtD) has a known role in pneumococcal Zn2+ homeostasis. However, the mechanistic basis of PhtD function remains unclear, partly due to a lack of structural information. Here, we determined the crystal structure of the fragment PhtD269-339 , containing the third Zn2+ -binding histidine triad (HT) motif of the protein. Analysis of the structure suggests that Zn2+ binding occurs at the surface of the protein and that all five HT motifs in the protein bind Zn2+ and share similar structures. These new structural insights aid in our understanding of how the Pht proteins facilitate pneumococcal Zn2+ acquisition.
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