Literature DB >> 23695577

Expression, purification and crystallization of the C-terminal LRR domain of Streptococcus pyogenes protein 0843.

Teemu Haikarainen1, Vuokko Loimaranta, Carlos Prieto-Lopez, Pradeep Battula, Jukka Finne, Anastassios C Papageorgiou.   

Abstract

Streptococcus pyogenes protein 0843 (Spy0843) is a recently identified protein with a potential adhesin function. Sequence analysis has shown that Spy0843 contains two leucine-rich repeat (LRR) domains that mediate interactions with the gp340 receptor. Here, the C-terminal LRR domain was overexpressed in Escherichia coli, purified and crystallized in the presence of 1.7-1.8 M ammonium sulfate pH 7.4 as precipitant. Data were collected from a single crystal to 1.59 Å resolution at 100 K at a synchrotron-radiation source. The crystal was found to belong to space group I41, with unit-cell parameters a = b = 121.4, c = 51.5 Å and one molecule in the asymmetric unit. Elucidation of the crystal structure will provide insights into the interactions of Spy0843 with the gp340 receptor and a better understanding of the role of Spy0843 in streptococcal infections.

Entities:  

Keywords:  Spy0843; Streptococcus pyogenes; bacterial adhesion; leucine-rich repeats; scavenger receptors

Mesh:

Substances:

Year:  2013        PMID: 23695577      PMCID: PMC3660901          DOI: 10.1107/S1744309113009664

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


  14 in total

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Authors:  V Loimaranta; N S Jakubovics; J Hytönen; J Finne; H F Jenkinson; N Strömberg
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10.  SMART 7: recent updates to the protein domain annotation resource.

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