 |
PDBsum entry 2y1v
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Structural protein
|
PDB id
|
|
|
|
2y1v
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
The full-Length streptococcus pneumoniae major pilin rrgb crystallizes in a fibre-Like structure, Which presents the d1 isopeptide bond and provides details on the mechanism of pilus polymerization.
|
|
|
Authors
|
|
L.El mortaji,
C.Contreras-Martel,
M.Moschioni,
I.Ferlenghi,
C.Manzano,
T.Vernet,
A.Dessen,
A.M.Di guilmi.
|
|
|
Ref.
|
|
Biochem J, 2012,
441,
833-841.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
RrgB is the major pilin which forms the pneumococcal pilus backbone. We report
the high-resolution crystal structure of the full-length form of RrgB containing
the IPQTG sorting motif. The RrgB fold is organized into four distinct domains,
D1-D4, each of which is stabilized by an isopeptide bond. Crystal packing
revealed a head-to-tail organization involving the interaction of the IPQTG
motif into the D1 domain of two successive RrgB monomers. This fibrillar
assembly, which fits into the electron microscopy density map of the native
pilus, probably induces the formation of the D1 isopeptide bond as observed for
the first time in the present study, since neither in published structures nor
in soluble RrgB produced in Escherichia coli or in Streptococcus pneumoniae is
the D1 bond present. Experiments performed in live bacteria confirmed that the
intermolecular bond linking the RrgB subunits takes place between the IPQTG
motif of one RrgB subunit and the Lys183 pilin motif residue of an adjacent RrgB
subunit. In addition, we present data indicating that the D1 isopeptide bond is
involved in RrgB stabilization. In conclusion, the crystal RrgB fibre is a
compelling model for deciphering the molecular details required to generate the
pneumococcal pilus.
|
|
|
|
|
|
|
