PDBsum entry 4g1h

Transferase

PDB id: 4g1h

Contents

Protein chain

176 a.a.

Metals

_CA

Waters ×91

PDB id:

4g1h

Name:

Transferase

Title:

Group b streptococcus pilus island 1 sortase c2

Structure:

Sortase family protein. Chain: a. Fragment: unp residues 19-233. Engineered: yes

Source:

Streptococcus agalactiae serogroup v. Organism_taxid: 216466. Gene: sag0648. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.80Å R-factor: 0.216 R-free: 0.251

Authors:

R.Cozzi,D.M.Prigozhin,T.Alber

Key ref:

R.Cozzi et al. (2012). Structural basis for group B streptococcus pilus 1 sortases C regulation and specificity. Plos One, 7, e49048. PubMed id: 23145064

Date:

10-Jul-12 Release date: 05-Dec-12

Protein chain

Q8E0S6  (Q8E0S6_STRA5) -  Sortase family protein from Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R)

Seq: 260 a.a.

Struc: 176 a.a.

Enzyme reactions

• Enzyme class: E.C.?

Plos One 7:e49048 (2012)

PubMed id: 23145064

Structural basis for group B streptococcus pilus 1 sortases C regulation and specificity.

R.Cozzi, D.Prigozhin, R.Rosini, F.Abate, M.J.Bottomley, G.Grandi, J.L.Telford, C.D.Rinaudo, D.Maione, T.Alber.

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.