3B2M

Crystal Structure of the Major Pilin from Streptococcus pyogenes

Summary for 3B2M

• Entry DOI: 10.2210/pdb3b2m/pdb
• Descriptor: Putative uncharacterized protein SPy0128 (2 entities in total)
• Functional Keywords: all-beta, pili, isopeptide, cell adhesion, structural protein
• Biological source: Streptococcus pyogenes serotype M1
• Cellular location: Secreted, cell wall; Peptidoglycan-anchor: Q9A1S2
• Total number of polymer chains: 3
• Total formula weight: 97440.01

Authors

Kang, H.J.,Coulibaly, F.,Proft, T.,Baker, E.N. (deposition date: 2007-10-18, release date: 2007-12-18, Last modification date: 2024-10-30)

Primary citation

Kang, H.J.,Coulibaly, F.,Clow, F.,Proft, T.,Baker, E.N.
Stabilizing isopeptide bonds revealed in gram-positive bacterial pilus structure.
Science, 318:1625-1628, 2007

PubMed Abstract: Many bacterial pathogens have long, slender pili through which they adhere to host cells. The crystal structure of the major pilin subunit from the Gram-positive human pathogen Streptococcus pyogenes at 2.2 angstroms resolution reveals an extended structure comprising two all-beta domains. The molecules associate in columns through the crystal, with each carboxyl terminus adjacent to a conserved lysine of the next molecule. This lysine forms the isopeptide bonds that link the subunits in native pili, validating the relevance of the crystal assembly. Each subunit contains two lysine-asparagine isopeptide bonds generated by an intramolecular reaction, and we find evidence for similar isopeptide bonds in other cell surface proteins of Gram-positive bacteria. The present structure explains the strength and stability of such Gram-positive pili and could facilitate vaccine development.

PubMed: 18063798
DOI: 10.1126/science.1145806

Experimental method

X-RAY DIFFRACTION (2.22 Å)