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Structural basis for group B streptococcus pilus 1 sortases C regulation and specificity.
- Source :
-
PloS one [PLoS One] 2012; Vol. 7 (11), pp. e49048. Date of Electronic Publication: 2012 Nov 08. - Publication Year :
- 2012
-
Abstract
- Gram-positive bacteria assemble pili through class C sortase enzymes specialized in polymerizing pilin subunits into covalently linked, high-molecular-weight, elongated structures. Here we report the crystal structures of two class C sortases (SrtC1 and SrtC2) from Group B Streptococcus (GBS) Pilus Island 1. The structures show that both sortases are comprised of two domains: an 8-stranded β-barrel catalytic core conserved among all sortase family members and a flexible N-terminal region made of two α-helices followed by a loop, known as the lid, which acts as a pseudo-substrate. In vitro experiments performed with recombinant SrtC enzymes lacking the N-terminal portion demonstrate that this region of the enzyme is dispensable for catalysis but may have key roles in substrate specificity and regulation. Moreover, in vitro FRET-based assays show that the LPXTG motif common to many sortase substrates is not the sole determinant of sortase C specificity during pilin protein recognition.
- Subjects :
- Catalysis
Catalytic Domain
Crystallography, X-Ray methods
Models, Molecular
Protein Folding
Protein Structure, Tertiary
Streptococcus chemistry
Substrate Specificity
Aminoacyltransferases chemistry
Bacterial Proteins chemistry
Cysteine Endopeptidases chemistry
Fimbriae Proteins chemistry
Fimbriae, Bacterial chemistry
Streptococcus enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 1932-6203
- Volume :
- 7
- Issue :
- 11
- Database :
- MEDLINE
- Journal :
- PloS one
- Publication Type :
- Academic Journal
- Accession number :
- 23145064
- Full Text :
- https://doi.org/10.1371/journal.pone.0049048