4y4q

Crystal structure of sortase B from Type II pilus of Streptococcus pneumoniae

spinqualitylabelsall models 4y4q, resolution 2.16Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4y4q is a 2 chain structure with sequence from Streptococcus pneumoniae PCS8235. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.162Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0M3KL14_STREE Publication Abstract from PubMed Pili are fibrous appendages expressed on the surface of a vast number of bacterial species, and their role in surface adhesion is important for processes such as infection, colonization, and biofilm formation. The human pathogen Streptococcus pneumoniae expresses two different types of pili, PI-1 and PI-2, both of which require the concerted action of structural proteins and sortases for their polymerization. The type PI-1 streptococcal pilus is a complex, well-studied structure, but the PI-2 type, present in a number of invasive pneumococcal serotypes, has to date remained less well understood. The PI-2 pilus consists of repeated units of a single protein, PitB, whose covalent association is catalyzed by cognate sortase SrtG-1 and partner protein SipA. Here we report the high-resolution crystal structures of PitB and SrtG1 and use molecular modeling to visualize a 'trapped' 1:1 complex between the two molecules. X-ray crystallography and electron microscopy reveal that the pneumococcal PI-2 backbone fiber is formed by PitB monomers associated in 'head-to-tail' fashion, and that short, flexible fibers can be formed even in the absence of coadjuvant proteins. These observations, obtained with a simple pilus biosynthetic system, are likely to be applicable to other fiber formation processes in a variety of Gram-positive organisms. A structural snapshot of type II pilus formation in Streptococcus pneumoniae.,Shaik MM, Lombardi C, Maragno Trindade D, Fenel D, Schoehn G, Di Guilmi AM, Dessen A J Biol Chem. 2015 Jul 21. pii: jbc.M115.647834. PMID:26198632 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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