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https://hdl.handle.net/2440/113416
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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 1873-3468 |
Statement of Responsibility: | 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 |
DOI: | 10.1002/1873-3468.13122 |
Grant ID: | http://purl.org/au-research/grants/arc/DP170102102 http://purl.org/au-research/grants/nhmrc/1071659 http://purl.org/au-research/grants/nhmrc/1080784 http://purl.org/au-research/grants/nhmrc/1122582 http://purl.org/au-research/grants/nhmrc/1110971 http://purl.org/au-research/grants/arc/FT170100006 |
Published version: | http://dx.doi.org/10.1002/1873-3468.13122 |
Appears in Collections: | Aurora harvest 8 Molecular and Biomedical Science publications |
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