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PDBsum entry 2ho1
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Protein binding
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PDB id
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2ho1
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Contents |
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* Residue conservation analysis
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J Bacteriol
190:6961-6969
(2008)
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PubMed id:
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PilF is an outer membrane lipoprotein required for multimerization and localization of the Pseudomonas aeruginosa Type IV pilus secretin.
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J.Koo,
S.Tammam,
S.Y.Ku,
L.M.Sampaleanu,
L.L.Burrows,
P.L.Howell.
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ABSTRACT
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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.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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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.
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Microbiology,
157,
1329-1342.
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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.
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Wound Repair Regen,
19,
214-222.
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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.
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Microb Pathog,
50,
293-302.
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S.Jain,
K.B.MoĊcicka,
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.
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PLoS One,
6,
e16624.
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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.
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Structure,
18,
265-273.
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PDB code:
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M.Ayers,
P.L.Howell,
and
L.L.Burrows
(2010).
Architecture of the type II secretion and type IV pilus machineries.
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Future Microbiol,
5,
1203-1218.
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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.
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J Bacteriol,
191,
6513-6524.
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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.
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J Bacteriol,
191,
898-908.
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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.
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Links
