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|Title:||Structural characterisation of the HT3 motif of the polyhistidine triad protein D from Streptococcus pneumoniae.|
|Citation:||FEBS Letters, 2018; 592(13):2341-2350|
|Zhenyao Luo, Victoria G. Pederick, James C. Paton, Christopher A. McDevitt and Bostjan Kobe|
|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. This article is protected by copyright. All rights reserved.|
|Keywords:||In situ proteolysis; PhtD; Polyhistidine triad; Streptococcus pneumoniae; X-ray crystallography; Zinc acquisition|
|Rights:||Copyright 2018 Federation of European Biochemical Societies|
|Appears in Collections:||Molecular and Biomedical Science publications|
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