3b2m
Crystal Structure of the Major Pilin from Streptococcus pyogenesCrystal Structure of the Major Pilin from Streptococcus pyogenes
Structural highlights
FunctionPILIN_STRP1 Major component of the pilus. A stack of the pilin subunits, joined by intermolecular isopeptide bonds, forms the pilus. The pilus is required for bacterial adhesion to host cells, for bacterial aggregation, and for biofilm formation.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMany 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. Stabilizing isopeptide bonds revealed in gram-positive bacterial pilus structure.,Kang HJ, Coulibaly F, Clow F, Proft T, Baker EN Science. 2007 Dec 7;318(5856):1625-8. PMID:18063798[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||