PDBsum entry 2ho1

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protein Protein-protein interface(s) links
Protein binding PDB id
Jmol PyMol
Protein chains
222 a.a. *
Waters ×314
* Residue conservation analysis
PDB id:
Name: Protein binding
Title: Functional characterization of pseudomonas aeruginosa pilf
Structure: Type 4 fimbrial biogenesis protein pilf. Chain: a, b. Engineered: yes
Source: Pseudomonas aeruginosa. Organism_taxid: 208964. Strain: pao1. Gene: pilf. Expressed in: escherichia coli. Expression_system_taxid: 562.
2.00Å     R-factor:   0.209     R-free:   0.248
Authors: J.Koo
Key ref: J.Koo et al. (2008). PilF is an outer membrane lipoprotein required for multimerization and localization of the Pseudomonas aeruginosa Type IV pilus secretin. J Bacteriol, 190, 6961-6969. PubMed id: 18776008
13-Jul-06     Release date:   25-Jul-06    
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Protein chains
Pfam   ArchSchema ?
Q9HXJ2  (Q9HXJ2_PSEAE) -  Type 4 fimbrial biogenesis protein PilF
252 a.a.
222 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     secretion   4 terms 
  Biochemical function     TPR domain binding     1 term  


J Bacteriol 190:6961-6969 (2008)
PubMed id: 18776008  
PilF is an outer membrane lipoprotein required for multimerization and localization of the Pseudomonas aeruginosa Type IV pilus secretin.
J.Koo, S.Tammam, S.Y.Ku, L.M.Sampaleanu, L.L.Burrows, P.L.Howell.
Type IV pili (T4P) are retractile appendages that contribute to the virulence of bacterial pathogens. PilF is a Pseudomonas aeruginosa lipoprotein that is essential for T4P biogenesis. Phenotypic characterization of a pilF mutant confirmed that T4P-mediated functions are abrogated: T4P were no longer present on the cell surface, twitching motility was abolished, and the mutant was resistant to infection by T4P retraction-dependent bacteriophage. The results of cellular fractionation studies indicated that PilF is the outer membrane pilotin required for the localization and multimerization of the secretin, PilQ. Mutation of the putative PilF lipidation site untethered the protein from the outer membrane, causing secretin assembly in both inner and outer membranes. T4P-mediated twitching motility and bacteriophage susceptibility were moderately decreased in the lipidation site mutant, while cell surface piliation was substantially reduced. The tethering of PilF to the outer membrane promotes the correct localization of PilQ and appears to be required for the formation of stable T4P. Our 2.0-A structure of PilF revealed a superhelical arrangement of six tetratricopeptide protein-protein interaction motifs that may mediate the contacts with PilQ during secretin assembly. An alignment of pseudomonad PilF sequences revealed three highly conserved surfaces that may be involved in PilF function.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21330432 A.V.Benam, E.Lång, K.Alfsnes, B.Fleckenstein, A.D.Rowe, E.Hovland, O.H.Ambur, S.A.Frye, and T.Tønjum (2011).
Structure-function relationships of the competence lipoprotein ComL and SSB in meningococcal transformation.
  Microbiology, 157, 1329-1342.  
21362089 G.Nakagami, T.Morohoshi, T.Ikeda, Y.Ohta, H.Sagara, L.Huang, T.Nagase, J.Sugama, and H.Sanada (2011).
Contribution of quorum sensing to the virulence of Pseudomonas aeruginosa in pressure ulcer infection in rats.
  Wound Repair Regen, 19, 214-222.  
21320583 L.Li, Z.Xu, Y.Zhou, T.Li, L.Sun, H.Chen, and R.Zhou (2011).
Analysis on Actinobacillus pleuropneumoniae LuxS regulated genes reveals pleiotropic roles of LuxS/AI-2 on biofilm formation, adhesion ability and iron metabolism.
  Microb Pathog, 50, 293-302.  
21304951 S.Jain, K.B.MoĊ›cicka, M.P.Bos, E.Pachulec, M.C.Stuart, W.Keegstra, E.J.Boekema, and C.van der Does (2011).
Structural Characterization of Outer Membrane Components of the Type IV Pili System in Pathogenic Neisseria.
  PLoS One, 6, e16624.  
20159471 C.L.Keiski, M.Harwich, S.Jain, A.M.Neculai, P.Yip, H.Robinson, J.C.Whitney, L.Riley, L.L.Burrows, D.E.Ohman, and P.L.Howell (2010).
AlgK is a TPR-containing protein and the periplasmic component of a novel exopolysaccharide secretin.
  Structure, 18, 265-273.
PDB code: 3e4b
20722599 M.Ayers, P.L.Howell, and L.L.Burrows (2010).
Architecture of the type II secretion and type IV pilus machineries.
  Future Microbiol, 5, 1203-1218.  
19717595 H.Harvey, M.Habash, F.Aidoo, and L.L.Burrows (2009).
Single-residue changes in the C-terminal disulfide-bonded loop of the Pseudomonas aeruginosa type IV pilin influence pilus assembly and twitching motility.
  J Bacteriol, 191, 6513-6524.  
19028883 J.Seo, A.Brencic, and A.J.Darwin (2009).
Analysis of secretin-induced stress in Pseudomonas aeruginosa suggests prevention rather than response and identifies a novel protein involved in secretin function.
  J Bacteriol, 191, 898-908.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.