Functional dissection of structural regions of the Here, we have used biochemical and genetic techniques to study the interaction of PilQ with PilW, a unique protein which is essential for natural transformation and T4P extrusion of T thermophilus PilQ and PilW form high molecular mass complexes in the OM of T thermophilus
RCSB PDB - 2VQ2: Crystal structure of PilW, widely conserved type IV . . . We report the high-resolution crystal structure of PilW, the partner lipoprotein of the type IV pilus secretin PilQ from Neisseria meningitidis, which defines a conserved class of Tfp biogenesis proteins involved in the formation and or stability of secretin multimers in a wide variety of bacteria
PlzR regulates type IV pili assembly in - Nature Here, Hendrix et al identify a protein that interacts with a T4P chaperone and inhibits pilus assembly and adsorption of T4P-dependent phages in Pseudomonas aeruginosa
PilY proteins: bimodular drivers of type IV pilus versatility PilY proteins are characterized by a shared domain architecture which consists of a variable N-terminal region that mediates adhesion and a conserved C-terminal beta-propeller domain that facilitates pilus biogenesis
Type IV pilus biogenesis factor PilY1 - UniProt Involved in pilus assembly, twitching motility and adhesion to host cells Primes type IV pili (T4P) assembly and is required for inclusion of minor pilins PilV, PilW and PilX to the surface pili (By similarity)