Structural characterisation of the HT3 motif of the polyhistidine triad protein D from Streptococcus pneumoniae.

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dc.contributor.authorLuo, Z.
dc.contributor.authorPederick, V.G.
dc.contributor.authorPaton, J.C.
dc.contributor.authorMcDevitt, C.A.
dc.contributor.authorKobe, B.
dc.date.issued2018
dc.description.abstractThe 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.
dc.description.statementofresponsibilityZhenyao Luo, Victoria G. Pederick, James C. Paton, Christopher A. McDevitt and Bostjan Kobe
dc.identifier.citationFEBS Letters, 2018; 592(13):2341-2350
dc.identifier.doi10.1002/1873-3468.13122
dc.identifier.issn0014-5793
dc.identifier.issn1873-3468
dc.identifier.orcidPaton, J.C. [0000-0001-9807-5278]
dc.identifier.orcidMcDevitt, C.A. [0000-0003-1596-4841]
dc.identifier.urihttp://hdl.handle.net/2440/113416
dc.language.isoen
dc.publisherWiley
dc.relation.granthttp://purl.org/au-research/grants/arc/DP170102102
dc.relation.granthttp://purl.org/au-research/grants/nhmrc/1071659
dc.relation.granthttp://purl.org/au-research/grants/nhmrc/1080784
dc.relation.granthttp://purl.org/au-research/grants/nhmrc/1122582
dc.relation.granthttp://purl.org/au-research/grants/nhmrc/1110971
dc.relation.granthttp://purl.org/au-research/grants/arc/FT170100006
dc.rightsCopyright 2018 Federation of European Biochemical Societies
dc.source.urihttps://doi.org/10.1002/1873-3468.13122
dc.subjectIn situ proteolysis
dc.subjectPhtD
dc.subjectPolyhistidine triad
dc.subjectStreptococcus pneumoniae
dc.subjectX-ray crystallography
dc.subjectZinc acquisition
dc.titleStructural characterisation of the HT3 motif of the polyhistidine triad protein D from Streptococcus pneumoniae.
dc.typeJournal article
pubs.publication-statusPublished

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