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* Residue conservation analysis
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PDB id:
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Signaling protein
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Title:
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Crystal structure of sifa and skip
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Structure:
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Protein sifa. Chain: a. Engineered: yes. Pleckstrin homology domain-containing family m member 2. Chain: b. Fragment: ph motif, unp residues 773-884. Synonym: salmonella-induced filaments a and kinesin-interacting protein, sifa and kinesin-interacting protein, skip. Engineered: yes
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Source:
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Salmonella typhimurium. Organism_taxid: 602. Gene: sifa, stm1224. Expressed in: escherichia coli. Expression_system_taxid: 562. Homo sapiens. Human. Organism_taxid: 9606. Gene: plekhm2, kiaa0842, skip.
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Resolution:
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2.60Å
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R-factor:
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0.258
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R-free:
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0.288
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Authors:
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Z.Huang,J.Chai
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Key ref:
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M.B.Ohlson
et al.
(2008).
Structure and function of Salmonella SifA indicate that its interactions with SKIP, SseJ, and RhoA family GTPases induce endosomal tubulation.
Cell Host Microbe,
4,
434-446.
PubMed id:
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Date:
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24-Apr-08
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Release date:
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02-Dec-08
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PROCHECK
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Headers
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References
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Enzyme class:
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Chains A, B:
E.C.?
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Cell Host Microbe
4:434-446
(2008)
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PubMed id:
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Structure and function of Salmonella SifA indicate that its interactions with SKIP, SseJ, and RhoA family GTPases induce endosomal tubulation.
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M.B.Ohlson,
Z.Huang,
N.M.Alto,
M.P.Blanc,
J.E.Dixon,
J.Chai,
S.I.Miller.
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ABSTRACT
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The Salmonella typhimurium type III secretion effector protein SifA is essential
for inducing tubulation of the Salmonella phagosome and binds the mammalian
kinesin-binding protein SKIP. Coexpression of SifA with the effector SseJ
induced tubulation of mammalian cell endosomes, similar to that induced by
Salmonella infection. Interestingly, GTP-bound RhoA, RhoB, and RhoC also induced
endosomal tubulation when coexpressed with SseJ, indicating that SifA likely
mimics or activates a RhoA family GTPase. The structure of SifA in complex with
the PH domain of SKIP revealed that SifA has two distinct domains; the amino
terminus binds SKIP, and the carboxyl terminus has a fold similar to SopE, a
Salmonella effector with Rho GTPase guanine nucleotide exchange factor activity
(GEF). Similar to GEFs, SifA interacted with GDP-bound RhoA, and purified SseJ
and RhoA formed a protein complex, suggesting that SifA, SKIP, SseJ, and RhoA
family GTPases cooperatively promote host membrane tubulation.
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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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J.E.Lillington,
J.E.Lovett,
S.Johnson,
P.Roversi,
C.R.Timmel,
and
S.M.Lea
(2011).
Shigella flexneri Spa15 crystal structure verified in solution by double electron electron resonance.
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J Mol Biol,
405,
427-435.
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PDB code:
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K.Aktories
(2011).
Bacterial protein toxins that modify host regulatory GTPases.
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Nat Rev Microbiol,
9,
487-498.
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Y.Litvak,
R.Levin-Klein,
M.Avner,
and
Z.Selinger
(2011).
High catalytic efficiency and resistance to denaturing in bacterial Rho GTPase-activating proteins.
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Biol Chem,
392,
505-516.
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A.Arbeloa,
J.Garnett,
J.Lillington,
R.R.Bulgin,
C.N.Berger,
S.M.Lea,
S.Matthews,
and
G.Frankel
(2010).
EspM2 is a RhoA guanine nucleotide exchange factor.
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Cell Microbiol,
12,
654-664.
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A.J.Müller,
C.Hoffmann,
and
W.D.Hardt
(2010).
Caspase-1 activation via Rho GTPases: a common theme in mucosal infections?
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PLoS Pathog,
6,
e1000795.
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B.A.Wilson,
and
M.Ho
(2010).
Recent insights into Pasteurella multocida toxin and other G-protein-modulating bacterial toxins.
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Future Microbiol,
5,
1185-1201.
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C.G.Moreira,
D.Weinshenker,
and
V.Sperandio
(2010).
QseC mediates Salmonella enterica serovar typhimurium virulence in vitro and in vivo.
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Infect Immun,
78,
914-926.
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C.V.Srikanth,
D.M.Wall,
A.Maldonado-Contreras,
H.N.Shi,
D.Zhou,
Z.Demma,
K.L.Mumy,
and
B.A.McCormick
(2010).
Salmonella pathogenesis and processing of secreted effectors by caspase-3.
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Science,
330,
390-393.
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D.B.Vinh,
D.C.Ko,
R.A.Rachubinski,
J.D.Aitchison,
and
S.I.Miller
(2010).
Expression of the Salmonella spp. virulence factor SifA in yeast alters Rho1 activity on peroxisomes.
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Mol Biol Cell,
21,
3567-3577.
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N.Dong,
L.Liu,
and
F.Shao
(2010).
A bacterial effector targets host DH-PH domain RhoGEFs and antagonizes macrophage phagocytosis.
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EMBO J,
29,
1363-1376.
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P.Cossart,
and
C.R.Roy
(2010).
Manipulation of host membrane machinery by bacterial pathogens.
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Curr Opin Cell Biol,
22,
547-554.
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R.Bulgin,
B.Raymond,
J.A.Garnett,
G.Frankel,
V.F.Crepin,
C.N.Berger,
and
A.Arbeloa
(2010).
Bacterial guanine nucleotide exchange factors SopE-like and WxxxE effectors.
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Infect Immun,
78,
1417-1425.
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R.J.Falconer,
A.Penkova,
I.Jelesarov,
and
B.M.Collins
(2010).
Survey of the year 2008: applications of isothermal titration calorimetry.
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J Mol Recognit,
23,
395-413.
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J.A.Ibarra,
and
O.Steele-Mortimer
(2009).
Salmonella--the ultimate insider. Salmonella virulence factors that modulate intracellular survival.
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Cell Microbiol,
11,
1579-1586.
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J.E.Galán
(2009).
Common themes in the design and function of bacterial effectors.
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Cell Host Microbe,
5,
571-579.
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L.Diacovich,
A.Dumont,
D.Lafitte,
E.Soprano,
A.A.Guilhon,
C.Bignon,
J.P.Gorvel,
Y.Bourne,
and
S.Méresse
(2009).
Interaction between the SifA virulence factor and its host target SKIP is essential for Salmonella pathogenesis.
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J Biol Chem,
284,
33151-33160.
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PDB code:
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N.C.Elde,
and
H.S.Malik
(2009).
The evolutionary conundrum of pathogen mimicry.
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Nat Rev Microbiol,
7,
787-797.
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Y.Kumar,
and
R.H.Valdivia
(2009).
Leading a sheltered life: intracellular pathogens and maintenance of vacuolar compartments.
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Cell Host Microbe,
5,
593-601.
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Z.Huang,
S.E.Sutton,
A.J.Wallenfang,
R.C.Orchard,
X.Wu,
Y.Feng,
J.Chai,
and
N.M.Alto
(2009).
Structural insights into host GTPase isoform selection by a family of bacterial GEF mimics.
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Nat Struct Mol Biol,
16,
853-860.
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PDB code:
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P.J.Hume,
and
V.Koronakis
(2008).
Mimicry is the sincerest form of flattery?
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Cell Host Microbe,
4,
411-412.
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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
