Luo, Z.Pederick, V.G.Paton, J.C.McDevitt, C.A.Kobe, B.2018-07-242018-07-242018FEBS Letters, 2018; 592(13):2341-23500014-57931873-3468http://hdl.handle.net/2440/113416The 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. This article is protected by copyright. All rights reserved.enCopyright 2018 Federation of European Biochemical SocietiesIn situ proteolysisPhtDPolyhistidine triadStreptococcus pneumoniaeX-ray crystallographyZinc acquisitionStructural characterisation of the HT3 motif of the polyhistidine triad protein D from Streptococcus pneumoniae.Journal article003009027210.1002/1873-3468.131220004387196000152-s2.0-85050109061424229Paton, J.C. [0000-0001-9807-5278]McDevitt, C.A. [0000-0003-1596-4841]