2Y1V

Full length structure of RrgB Pilus protein from Streptococcus pneumoniae

Summary for 2Y1V

• Entry DOI: 10.2210/pdb2y1v/pdb
• Related: 2X9W 2X9X 2X9Y 2X9Z
• Descriptor: CELL WALL SURFACE ANCHOR FAMILY PROTEIN, NICKEL (II) ION (3 entities in total)
• Functional Keywords: structural protein, major pilin, pilus assembly
• Biological source: STREPTOCOCCUS PNEUMONIAE
• Total number of polymer chains: 3
• Total formula weight: 196604.25

Authors

El-Mortaji, L.,Contreras-Martel, C.,Manzano, C.,Vernet, T.,Dessen, A.,DiGuilmi, A.M. (deposition date: 2010-12-10, release date: 2011-11-09, Last modification date: 2024-10-16)

Primary citation

El Mortaji, L.,Contreras-Martel, C.,Moschioni, M.,Ferlenghi, I.,Manzano, C.,Vernet, T.,Dessen, A.,Di Guilmi, A.M.
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.
Biochem.J., 441:833-, 2012

PubMed 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.

PubMed: 22013894
DOI: 10.1042/BJ20111397

Experimental method

X-RAY DIFFRACTION (2.39 Å)