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Structural characterisation of the HT3 motif of the polyhistidine triad protein D from Streptococcus pneumoniae
Author(s) -
Luo Zhenyao,
Pederick Victoria G.,
Paton James C.,
McDevitt Christopher A.,
Kobe Bostjan
Publication year - 2018
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13122
Subject(s) - streptococcus pneumoniae , histidine , virulence , bacterial protein , protein structure , triad (sociology) , pathogen , biology , computational biology , human pathogen , chemistry , biochemistry , bacteria , microbiology and biotechnology , genetics , amino acid , gene , psychology , psychoanalysis
The bacterium Streptococcus pneumoniae (the pneumococcus) is a major human pathogen that requires Zn 2+ for its survival and virulence in the host environment. Polyhistidine triad protein D (PhtD) has a known role in pneumococcal Zn 2+ 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 PhtD 269‐339 , containing the third Zn 2+ ‐binding histidine triad (HT) motif of the protein. Analysis of the structure suggests that Zn 2+ binding occurs at the surface of the protein and that all five HT motifs in the protein bind Zn 2+ and share similar structures. These new structural insights aid in our understanding of how the Pht proteins facilitate pneumococcal Zn 2+ acquisition.