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Type: Journal article
Title: Heterogeneous nucleation is required for crystallization of the ZnuA domain of pneumococcal AdcA
Author: Luo, Z.
Morey, J.
McDevitt, C.
Kobe, B.
Citation: Acta Crystallographica Section F: Structural Biology Communications, 2015; 71(Pt 12):1459-1464
Publisher: International Union of Crystallography
Issue Date: 2015
ISSN: 2053-230X
Statement of
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
RMID: 0030040432
DOI: 10.1107/S2053230X15021330
Grant ID:
Appears in Collections:Molecular and Biomedical Science publications

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