Please use this identifier to cite or link to this item:
|Scopus||Web of Science®||Altmetric|
|Title:||Heterogeneous nucleation is required for crystallization of the ZnuA domain of pneumococcal AdcA|
|Citation:||Acta Crystallographica Section F: Structural Biology Communications, 2015; 71(Pt 12):1459-1464|
|Publisher:||International Union of Crystallography|
|Z. Luo, J. R. Morey, C. A. McDevitt and B. Kobe|
|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 the heterogeneous nucleating agent. These initial crystals were subsequently used as seeds to produce diffraction-quality crystals. The crystals diffracted to 2.03 Å resolution and had the symmetry of space group P1. This study demonstrates the utility of heterogeneous nucleation. The solution of the crystal structures will lead to further understanding of Zn²⁺ acquisition by S. pneumoniae.|
|Keywords:||AdcA; Streptococcus pneumoniae; Zn2+; ZnuA; heterogeneous nucleation; seaweed; solute-binding protein|
|Rights:||© International Union of Crystallography|
|Appears in Collections:||Molecular and Biomedical Science publications|
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.