Literature DB >> 20823536

Preliminary crystallographic study of the Streptococcus agalactiae sortases, sortase A and sortase C1.

Baldeep Khare1, Alexandra Samal, Krishnan Vengadesan, K R Rajashankar, Xin Ma, I Hsiu Huang, Hung Ton-That, Sthanam V L Narayana.   

Abstract

Sortases are cysteine transpeptidases that are essential for the assembly and anchoring of cell-surface adhesins in Gram-positive bacteria. In Streptococcus agalactiae (GBS), the pilin-specific sortase SrtC1 catalyzes the polymerization of pilins encoded by pilus island 1 (PI-1) and the housekeeping sortase SrtA is necessary for cell-wall anchoring of the resulting pilus polymers. These sortases are known to utilize different substrates for pilus polymerization and cell-wall anchoring; however, the structural correlates that dictate their substrate specificity have not yet been clearly defined. This report presents the expression, purification and crystallization of SrtC1 (SAG0647) and SrtA (SAG0961) from S. agalactiae strain 2603V/R. The GBS SrtC1 has been crystallized in three crystal forms and the GBS SrtA has been crystallized in one crystal form.

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Year:  2010        PMID: 20823536      PMCID: PMC2935237          DOI: 10.1107/S1744309110031106

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


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  4 in total

1.  The crystal structure analysis of group B Streptococcus sortase C1: a model for the "lid" movement upon substrate binding.

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2.  A model for group B Streptococcus pilus type 1: the structure of a 35-kDa C-terminal fragment of the major pilin GBS80.

Authors:  Krishnan Vengadesan; Xin Ma; Prabhat Dwivedi; Hung Ton-That; Sthanam V L Narayana
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3.  Structural and biochemical analyses of selectivity determinants in chimeric Streptococcus Class A sortase enzymes.

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4.  Structural differences between the Streptococcus agalactiae housekeeping and pilus-specific sortases: SrtA and SrtC1.

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