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Heterogeneous nucleation is required for crystallization of the ZnuA domain of pneumococcal AdcA
Author(s) -
Luo Zhenyao,
Morey Jacqueline R.,
McDevitt Christopher A.,
Kobe Boštjan
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15021330
Subject(s) - crystallization , nucleation , domain (mathematical analysis) , mathematics , physics , thermodynamics , mathematical analysis
Zn 2+ is an essential nutrient for all known forms of life. In the major human pathogen Streptococcus pneumoniae , the acquisition of Zn 2+ is facilitated by two Zn 2+ ‐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 Zn 2+ 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 P 1. This study demonstrates the utility of heterogeneous nucleation. The solution of the crystal structures will lead to further understanding of Zn 2+ acquisition by S. pneumoniae .