2X9X

STRUCTURE OF THE PILUS BACKBONE (RRGB) FROM STREPTOCOCCUS PNEUMONIAE

Summary for 2X9X

• Entry DOI: 10.2210/pdb2x9x/pdb
• Related: 2X9W 2X9Y 2X9Z
• Descriptor: CELL WALL SURFACE ANCHOR FAMILY PROTEIN, IMIDAZOLE, SODIUM ION, ... (4 entities in total)
• Functional Keywords: cell adhesion
• Biological source: STREPTOCOCCUS PNEUMONIAE
• Total number of polymer chains: 1
• Total formula weight: 48302.16

Authors

Spraggon, G.,Koesema, E.,Scarselli, M.,Malito, E.,Biagini, M.,Norais, N.,Emolo, C.,Barocchi, M.A.,Giusti, F.,Hilleringmann, M.,Rappuoli, R.,Lesley, S.,Covacci, A.,Masignani, V.,Ferlenghi, I. (deposition date: 2010-03-25, release date: 2010-06-30, Last modification date: 2024-10-23)

Primary citation

Spraggon, G.,Koesema, E.,Scarselli, M.,Malito, E.,Biagini, M.,Norais, N.,Emolo, C.,Barocchi, M.A.,Giusti, F.,Hilleringmann, M.,Rappuoli, R.,Lesley, S.,Covacci, A.,Masignani, V.,Ferlenghi, I.
Supramolecular Organization of the Repetitive Backbone Unit of the Streptococcus Pneumoniae Pilus.
Plos One, 5:919-, 2010

PubMed Abstract: Streptococcus pneumoniae, like many other Gram-positive bacteria, assembles long filamentous pili on their surface through which they adhere to host cells. Pneumococcal pili are formed by a backbone, consisting of the repetition of the major component RrgB, and two accessory proteins (RrgA and RrgC). Here we reconstruct by transmission electron microscopy and single particle image reconstruction method the three dimensional arrangement of two neighbouring RrgB molecules, which represent the minimal repetitive structural domain of the native pilus. The crystal structure of the D2-D4 domains of RrgB was solved at 1.6 A resolution. Rigid-body fitting of the X-ray coordinates into the electron density map enabled us to define the arrangement of the backbone subunits into the S. pneumoniae native pilus. The quantitative fitting provide evidence that the pneumococcal pilus consists uniquely of RrgB monomers assembled in a head-to-tail organization. The presence of short intra-subunit linker regions connecting neighbouring domains provides the molecular basis for the intrinsic pilus flexibility.

PubMed: 20559564
DOI: 10.1371/JOURNAL.PONE.0010919

Experimental method

X-RAY DIFFRACTION (1.5 Å)