title: Redefining the PF06864 Pfam family based on Burkholderia pseudomallei PilO2(Bp) S-SAD crystal structure.
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 PilO2(Bp), a protein component of the Tfpb R64 thin pilus variant assembly machinery from the pathogen Burkholderia pseudomallei. PilO2(Bp) 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 N-terminal domain of PilO2(Bp) (N-PilO2(Bp)), here reported, is the first structural representative of the PF06864 family. N-PilO2(Bp) 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.
authors.affiliation: Department of Biosciences, University of Milan, Milan, Italy.
authors.forename: Patricia
authors.initials: P
authors.lastname: Lassaux
authors.affiliation: Institute of Biotechnology and Biomedicine, Universitat Autònoma de Barcelona, Bellaterra, Spain.
authors.forename: Oscar
authors.initials: O
authors.lastname: Conchillo-Solé
authors.affiliation: European Molecular Biology Laboratory, Grenoble Outstation, Grenoble, France; Unit for Virus Host-Cell Interactions, Université Grenoble Alpes- European Molecular Biology Laboratory-Centre National de la Recherche Scientifique, Grenoble, France.
authors.forename: Babu A
authors.initials: BA
authors.lastname: Manjasetty
authors.affiliation: Institute of Biotechnology and Biomedicine, Universitat Autònoma de Barcelona, Bellaterra, Spain.
authors.forename: Daniel
authors.initials: D
authors.lastname: Yero
authors.affiliation: Department of Biosciences, University of Milan, Milan, Italy.
authors.forename: Lucia
authors.initials: L
authors.lastname: Perletti
authors.affiliation: European Molecular Biology Laboratory, Grenoble Outstation, Grenoble, France; Unit for Virus Host-Cell Interactions, Université Grenoble Alpes- European Molecular Biology Laboratory-Centre National de la Recherche Scientifique, Grenoble, France.
authors.forename: Hassan
authors.initials: H
authors.lastname: Belrhali
authors.affiliation: Institute of Biotechnology and Biomedicine, Universitat Autònoma de Barcelona, Bellaterra, Spain; Catalan Institution for Research and Advanced Studies, Barcelona, Spain.
authors.forename: Xavier
authors.initials: X
authors.lastname: Daura
authors.affiliation: Department of Biosciences, University of Milan, Milan, Italy.
authors.forename: Louise J
authors.initials: LJ
authors.lastname: Gourlay
authors.affiliation: Department of Biosciences, University of Milan, Milan, Italy; Interdisciplinary Centre for Nanostructured Materials and Interfaces and Consiglio Nazionale delle Ricerche, Institute of Biophysics, c/o University of Milan, Milan, Italy.
authors.forename: Martino
authors.initials: M
authors.lastname: Bolognesi
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D016957:Burkholderia pseudomallei / Q000235:genetics* / Q000378:metabolism*; D023061:Gene Order; D008958:Models, Molecular; D005810:Multigene Family; D009876:Operon; D011487:Protein Conformation; D017510:Protein Folding; D054730:Protein Interaction Domains and Motifs; D037521:Virulence Factors
chemical_list: D001426:Bacterial Proteins; D037521:Virulence Factors
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