Journal article

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

Zhenyao Luo, Victoria G Pederick, James C Paton, Christopher A McDevitt, Bostjan Kobe

FEBS LETTERS | WILEY | Published : 2018

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 structu..

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Grants

Awarded by National Health and Medical Research Council (NHMRC)


Awarded by ARC


Funding Acknowledgements

We acknowledge the use of the UQ-ROCX Facility and the Australian Synchrotron MX beamlines. This work was supported by the National Health and Medical Research Council (NHMRC) Program Grant 1071659 to BK and JCP and Project Grants 1080784 and 1122582 to CAM. This work was also supported by the ARC Discovery Project DP170102102 to CAM and JCP. CAM is an ARC Future Fellow (FT170100006) and BK is an NHMRC Principal Research Fellow (1110971).