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Type: Journal article
Title: Structural characterisation of the HT3 motif of the polyhistidine triad protein D from Streptococcus pneumoniae.
Author: Luo, Z.
Pederick, V.G.
Paton, J.C.
McDevitt, C.A.
Kobe, B.
Citation: FEBS Letters, 2018; 592(13):2341-2350
Publisher: Wiley
Issue Date: 2018
ISSN: 0014-5793
Statement of
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
Polyhistidine triad
Streptococcus pneumoniae
X-ray crystallography
Zinc acquisition
Rights: Copyright 2018 Federation of European Biochemical Societies
DOI: 10.1002/1873-3468.13122
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Appears in Collections:Aurora harvest 8
Molecular and Biomedical Science publications

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