Single-residue changes in the C-terminal disulfide-bonded loop of the Pseudomonas aeruginosa type IV pilin influence pilus assembly and twitching motility.

Abstract excerpt

PilA, the major pilin subunit of Pseudomonas aeruginosa type IV pili (T4P), is a principal structural component. PilA has a conserved C-terminal disulfide-bonded loop (DSL) that has been implicated as the pilus adhesinotope. Structural studies have suggested that DSL is involved in intersubunit interactions within the pilus fiber. PilA mutants with single-residue substitutions, insertions, or deletions in the DSL...

Topics

• Amino Acid Motifs
• Amino Acid Sequence
• Fimbriae Proteins
• Gene Expression Regulation, Bacterial
• Models, Molecular
• Mutation
• Phenotype
• Protein Conformation
• Protein Subunits
• Pseudomonas aeruginosa