7ba2

D319A mutant of the PilB minor pilin from Streptococcus sanguinisD319A mutant of the PilB minor pilin from Streptococcus sanguinis

Structural highlights 7ba2 is a 2 chain structure with sequence from Streptococcus sanguinis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0B7GP99_STRSA Required for transformation and DNA binding.[ARBA:ARBA00003988] Publication Abstract from PubMed Type IV pili (T4P) are functionally versatile filamentous nanomachines, nearly ubiquitous in prokaryotes. They are predominantly polymers of one major pilin but also contain minor pilins whose functions are often poorly defined and likely to be diverse. Here, we show that the minor pilin PilB from the T4P of Streptococcus sanguinis displays an unusual bimodular three-dimensional structure with a bulky von Willebrand factor A-like (vWA) module "grafted" onto a small pilin module via a short loop. Structural modeling suggests that PilB is only compatible with a localization at the tip of T4P. By performing a detailed functional analysis, we found that 1) the vWA module contains a canonical metal ion-dependent adhesion site, preferentially binding Mg(2+) and Mn(2+), 2) abolishing metal binding has no impact on the structure of PilB or piliation, 3) metal binding is important for S. sanguinis T4P-mediated twitching motility and adhesion to eukaryotic cells, and 4) the vWA module shows an intrinsic binding ability to several host proteins. These findings reveal an elegant yet simple evolutionary tinkering strategy to increase T4P functional versatility by grafting a functional module onto a pilin for presentation by the filaments. This strategy appears to have been extensively used by bacteria, in which modular pilins are widespread and exhibit an astonishing variety of architectures. PilB from Streptococcus sanguinis is a bimodular type IV pilin with a direct role in adhesion.,Raynaud C, Sheppard D, Berry JL, Gurung I, Pelicic V Proc Natl Acad Sci U S A. 2021 Jun 1;118(22). pii: 2102092118. doi:, 10.1073/pnas.2102092118. PMID:34031252 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pilin 3D structures

spinqualitylabelsall models 7ba2, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image