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PDBsum entry 4g1h
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References listed in PDB file
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Key reference
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Title
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Structural basis for group b streptococcus pilus 1 sortases c regulation and specificity.
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Authors
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R.Cozzi,
D.Prigozhin,
R.Rosini,
F.Abate,
M.J.Bottomley,
G.Grandi,
J.L.Telford,
C.D.Rinaudo,
D.Maione,
T.Alber.
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Ref.
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Plos One, 2012,
7,
e49048.
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PubMed id
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Abstract
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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.
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