Redefining the PF06864 pfam family based on burkholderia pseudomallei PilO2<inf>Bp</inf> S-SAD crystal structure

Patricia Lassaux, Oscar Conchillo-Solé, Babu A. Manjasetty, Daniel Yero, Lucia Perletti, Hassan Belrhali, Xavier Daura, Louise J. Gourlay, Martino Bolognesi

Research output: Contribution to journalArticleResearchpeer-review

4 Citations (Scopus)

Abstract

Type IV pili are surface-exposed filaments and bacterial virulence factors, represented by the Tfpa and Tfpb types, which assemble via specific machineries. The Tfpb group is further divided into seven variants, linked to heterogeneity in the assembly machineries. Here we focus on PilO2Bp, a protein component of the Tfpb R64 thin pilus variant assembly machinery from the pathogen Burkholderia pseudomallei. PilO2Bp belongs to the PF06864 Pfam family, for which an improved definition is presented based on newly derived Hidden Markov Model (HMM) profiles. The 3D structure of the Nterminal domain of PilO2Bp (N-PilO2Bp), here reported, is the first structural representative of the PF06864 family. N-PilO2Bp presents an actin-like ATPase fold that is shown to be present in BfpC, a different variant assembly protein; the new HMM profiles classify BfpC as a PF06864 member. Our results provide structural insight into the PF06864 family and on the Type IV pili assembly machinery. © 2014 Lassaux et al.
Original languageEnglish
Article numbere94981
JournalPLoS ONE
Volume9
DOIs
Publication statusPublished - 11 Apr 2014

Fingerprint Dive into the research topics of 'Redefining the PF06864 pfam family based on burkholderia pseudomallei PilO2<inf>Bp</inf> S-SAD crystal structure'. Together they form a unique fingerprint.

Cite this