4G1J

Sortase C1 of GBS Pilus Island 1

Summary for 4G1J

• Entry DOI: 10.2210/pdb4g1j/pdb
• Related: 4G1H
• Descriptor: Sortase family protein (2 entities in total)
• Functional Keywords: cysteine protease, extracellular, transferase
• Biological source: Streptococcus agalactiae serogroup V
• Total number of polymer chains: 2
• Total formula weight: 49636.41

Authors

Cozzi, R.,Prigozhin, D.M.,Alber, T. (deposition date: 2012-07-10, release date: 2012-12-05, Last modification date: 2024-02-28)

Primary citation

Cozzi, R.,Prigozhin, D.,Rosini, R.,Abate, F.,Bottomley, M.J.,Grandi, G.,Telford, J.L.,Rinaudo, C.D.,Maione, D.,Alber, T.
Structural basis for group B streptococcus pilus 1 sortases C regulation and specificity.
Plos One, 7:e49048-e49048, 2012

PubMed 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.

PubMed: 23145064
DOI: 10.1371/journal.pone.0049048

Experimental method

X-RAY DIFFRACTION (1.75 Å)