Journal article

Heterogeneous nucleation is required for crystallization of the ZnuA domain of pneumococcal AdcA

Z Luo, JR Morey, CA McDevitt, B Kobe

Acta Crystallographica Section F Structural Biology Communications | INT UNION CRYSTALLOGRAPHY | Published : 2015

Abstract

Zn2+ is an essential nutrient for all known forms of life. In the major human pathogen Streptococcus pneumoniae, the acquisition of Zn2+ is facilitated by two Zn2+-specific solute-binding proteins: AdcA and AdcAII. To date, there has been a paucity of structural information on AdcA, which has hindered a deeper understanding of the mechanism underlying pneumococcal Zn2+ acquisition. Native AdcA consists of two domains: an N-terminal ZnuA domain and a C-terminal ZinT domain. In this study, the ZnuA domain of AdcA was crystallized. The initial crystals of the ZnuA-domain protein were obtained using dried seaweed as a heterogeneous nucleating agent. No crystals were obtained in the absence of th..

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University of Melbourne Researchers

Grants

Awarded by National Health and Medical Research Council of Australia (NHMRC)


Awarded by Australian Research Council


Funding Acknowledgements

We acknowledge the use of the Australian Synchrotron MX beamlines and the UQ-ROCX Facility. We also thank Alastair McEwan and Rafael Counago for helpful discussions and for critical review of the manuscript. This work was supported by the National Health and Medical Research Council of Australia (NHMRC) Program grants 565526 and 1071659 to BK and Project grants 1022240 and 1080784 to CAM and the Australian Research Council Discovery Project Grants DP120103957 and DP150101856 to CAM. BK is an NHMRC Research Fellow (1003326).