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PDBsum entry 1tyu
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Viral adhesion protein
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PDB id
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1tyu
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Proc Natl Acad Sci U S A
93:10584-10588
(1996)
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PubMed id:
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Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors.
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S.Steinbacher,
U.Baxa,
S.Miller,
A.Weintraub,
R.Seckler,
R.Huber.
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ABSTRACT
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The O-antigenic repeating units of lipopolysaccharides from Salmonella
serogroups A, B, and D1 serve as receptors for the phage P22 tailspike protein,
which also has receptor destroying endoglycosidase (endorhamnosidase) activity,
integrating the functions of both hemagglutinin and neuraminidase in influenza
virus. Crystal structures of the tailspike protein in complex with
oligosaccharides, comprising two O-antigenic repeating units from Salmonella
typhimurium, Salmonella enteritidis, and Salmonella typhi 253Ty were determined
at 1.8 A resolution. The active-site topology with Asp-392, Asp-395, and Glu-359
as catalytic residues was identified. Kinetics of binding and cleavage suggest a
role of the receptor destroying endorhamnosidase activity primarily for
detachment of newly assembled phages.
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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.Tang,
G.C.Lander,
A.Olia,
R.Li,
S.Casjens,
P.Prevelige,
G.Cingolani,
T.S.Baker,
and
J.E.Johnson
(2011).
Peering down the barrel of a bacteriophage portal: the genome packaging and release valve in p22.
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Structure,
19,
496-502.
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A.Nalbantsoy,
I.Karaboz,
and
I.D.Gurhan
(2010).
Production of monoclonal antibodies in a mouse model via lipopolysaccharide conjugates with synthetic polymers specific to Salmonella Enteritidis O antigen.
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Foodborne Pathog Dis,
7,
1521-1529.
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M.Biancalana,
K.Makabe,
and
S.Koide
(2010).
Minimalist design of water-soluble cross-{beta} architecture.
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Proc Natl Acad Sci U S A,
107,
3469-3474.
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PDB codes:
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P.Firozi,
W.Zhang,
L.Chen,
F.A.Quiocho,
K.C.Worley,
and
N.S.Templeton
(2010).
Identification and removal of colanic acid from plasmid DNA preparations: implications for gene therapy.
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Gene Ther,
17,
1484-1499.
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S.Waseh,
P.Hanifi-Moghaddam,
R.Coleman,
M.Masotti,
S.Ryan,
M.Foss,
R.MacKenzie,
M.Henry,
C.M.Szymanski,
and
J.Tanha
(2010).
Orally administered P22 phage tailspike protein reduces salmonella colonization in chickens: prospects of a novel therapy against bacterial infections.
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PLoS One,
5,
e13904.
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A.Bhardwaj,
N.Walker-Kopp,
S.R.Casjens,
and
G.Cingolani
(2009).
An evolutionarily conserved family of virion tail needles related to bacteriophage P22 gp26: correlation between structural stability and length of the alpha-helical trimeric coiled coil.
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J Mol Biol,
391,
227-245.
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D.Schwarzer,
K.Stummeyer,
T.Haselhorst,
F.Freiberger,
B.Rode,
M.Grove,
T.Scheper,
M.von Itzstein,
M.Mühlenhoff,
and
R.Gerardy-Schahn
(2009).
Proteolytic release of the intramolecular chaperone domain confers processivity to endosialidase F.
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J Biol Chem,
284,
9465-9474.
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G.C.Lander,
R.Khayat,
R.Li,
P.E.Prevelige,
C.S.Potter,
B.Carragher,
and
J.E.Johnson
(2009).
The P22 tail machine at subnanometer resolution reveals the architecture of an infection conduit.
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Structure,
17,
789-799.
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C.Wasmer,
A.Lange,
H.Van Melckebeke,
A.B.Siemer,
R.Riek,
and
B.H.Meier
(2008).
Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core.
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Science,
319,
1523-1526.
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PDB code:
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J.J.Müller,
S.Barbirz,
K.Heinle,
A.Freiberg,
R.Seckler,
and
U.Heinemann
(2008).
An intersubunit active site between supercoiled parallel beta helices in the trimeric tailspike endorhamnosidase of Shigella flexneri Phage Sf6.
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Structure,
16,
766-775.
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PDB codes:
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J.Landström,
E.L.Nordmark,
R.Eklund,
A.Weintraub,
R.Seckler,
and
G.Widmalm
(2008).
Interaction of a Salmonella enteritidis O-antigen octasaccharide with the phage P22 tailspike protein by NMR spectroscopy and docking studies.
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Glycoconj J,
25,
137-143.
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K.H.Choi,
J.McPartland,
I.Kaganman,
V.D.Bowman,
L.B.Rothman-Denes,
and
M.G.Rossmann
(2008).
Insight into DNA and protein transport in double-stranded DNA viruses: the structure of bacteriophage N4.
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J Mol Biol,
378,
726-736.
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P.G.Leiman,
and
I.J.Molineux
(2008).
Evolution of a new enzyme activity from the same motif fold.
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Mol Microbiol,
69,
287-290.
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S.Barbirz,
J.J.Müller,
C.Uetrecht,
A.J.Clark,
U.Heinemann,
and
R.Seckler
(2008).
Crystal structure of Escherichia coli phage HK620 tailspike: podoviral tailspike endoglycosidase modules are evolutionarily related.
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Mol Microbiol,
69,
303-316.
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PDB codes:
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S.R.Casjens
(2008).
Diversity among the tailed-bacteriophages that infect the Enterobacteriaceae.
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Res Microbiol,
159,
340-348.
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J.E.Johnson,
and
W.Chiu
(2007).
DNA packaging and delivery machines in tailed bacteriophages.
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Curr Opin Struct Biol,
17,
237-243.
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A.V.McDonnell,
M.Menke,
N.Palmer,
J.King,
L.Cowen,
and
B.Berger
(2006).
Fold recognition and accurate sequence-structure alignment of sequences directing beta-sheet proteins.
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Proteins,
63,
976-985.
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R.Simkovsky,
and
J.King
(2006).
An elongated spine of buried core residues necessary for in vivo folding of the parallel beta-helix of P22 tailspike adhesin.
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Proc Natl Acad Sci U S A,
103,
3575-3580.
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R.Stern,
and
M.J.Jedrzejas
(2006).
Hyaluronidases: their genomics, structures, and mechanisms of action.
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Chem Rev,
106,
818-839.
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C.Etchebest,
C.Benros,
S.Hazout,
and
A.G.de Brevern
(2005).
A structural alphabet for local protein structures: improved prediction methods.
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Proteins,
59,
810-827.
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L.Tang,
W.R.Marion,
G.Cingolani,
P.E.Prevelige,
and
J.E.Johnson
(2005).
Three-dimensional structure of the bacteriophage P22 tail machine.
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EMBO J,
24,
2087-2095.
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R.Villafane,
S.Costa,
R.Ahmed,
and
C.Salgado
(2005).
Conservation of the N-terminus of some phage tail proteins.
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Arch Virol,
150,
2609-2621.
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S.A.Douthit,
M.Dlakic,
D.E.Ohman,
and
M.J.Franklin
(2005).
Epimerase active domain of Pseudomonas aeruginosa AlgG, a protein that contains a right-handed beta-helix.
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J Bacteriol,
187,
4573-4583.
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I.R.Henderson,
F.Navarro-Garcia,
M.Desvaux,
R.C.Fernandez,
and
D.Ala'Aldeen
(2004).
Type V protein secretion pathway: the autotransporter story.
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Microbiol Mol Biol Rev,
68,
692-744.
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S.Betts,
C.Haase-Pettingell,
K.Cook,
and
J.King
(2004).
Buried hydrophobic side-chains essential for the folding of the parallel beta-helix domains of the P22 tailspike.
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Protein Sci,
13,
2291-2303.
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W.Rabsch,
R.A.Helm,
and
A.Eisenstark
(2004).
Diversity of phage types among archived cultures of the Demerec collection of Salmonella enterica serovar Typhimurium strains.
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Appl Environ Microbiol,
70,
664-669.
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M.A.McDonough,
C.Ryttersgaard,
M.E.Bjørnvad,
L.Lo Leggio,
M.Schülein,
S.O.Schrøder Glad,
and
S.Larsen
(2002).
Crystallization and preliminary X-ray characterization of a thermostable pectate lyase from Thermotoga maritima.
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Acta Crystallogr D Biol Crystallogr,
58,
709-711.
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A.V.Kajava,
N.Cheng,
R.Cleaver,
M.Kessel,
M.N.Simon,
E.Willery,
F.Jacob-Dubuisson,
C.Locht,
and
A.C.Steven
(2001).
Beta-helix model for the filamentous haemagglutinin adhesin of Bordetella pertussis and related bacterial secretory proteins.
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Mol Microbiol,
42,
279-292.
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C.Haase-Pettingell,
S.Betts,
S.W.Raso,
L.Stuart,
A.Robinson,
and
J.King
(2001).
Role for cysteine residues in the in vivo folding and assembly of the phage P22 tailspike.
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Protein Sci,
10,
397-410.
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P.Bradley,
L.Cowen,
M.Menke,
J.King,
and
B.Berger
(2001).
BETAWRAP: successful prediction of parallel beta -helices from primary sequence reveals an association with many microbial pathogens.
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Proc Natl Acad Sci U S A,
98,
14819-14824.
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U.Dengler,
A.S.Siddiqui,
and
G.J.Barton
(2001).
Protein structural domains: analysis of the 3Dee domains database.
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Proteins,
42,
332-344.
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B.Schuler,
F.Fürst,
F.Osterroth,
S.Steinbacher,
R.Huber,
and
R.Seckler
(2000).
Plasticity and steric strain in a parallel beta-helix: rational mutations in the P22 tailspike protein.
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Proteins,
39,
89.
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PDB codes:
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J.F.Kreisberg,
S.D.Betts,
and
J.King
(2000).
Beta-helix core packing within the triple-stranded oligomerization domain of the P22 tailspike.
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Protein Sci,
9,
2338-2343.
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R.Kuroki,
L.H.Weaver,
and
B.W.Matthews
(1999).
Structural basis of the conversion of T4 lysozyme into a transglycosidase by reengineering the active site.
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Proc Natl Acad Sci U S A,
96,
8949-8954.
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PDB codes:
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S.Betts,
and
J.King
(1999).
There's a right way and a wrong way: in vivo and in vitro folding, misfolding and subunit assembly of the P22 tailspike.
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Structure,
7,
R131-R139.
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S.D.Betts,
and
J.King
(1998).
Cold rescue of the thermolabile tailspike intermediate at the junction between productive folding and off-pathway aggregation.
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Protein Sci,
7,
1516-1523.
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S.Miller,
B.Schuler,
and
R.Seckler
(1998).
A reversibly unfolding fragment of P22 tailspike protein with native structure: the isolated beta-helix domain.
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Biochemistry,
37,
9160-9168.
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S.Miller,
B.Schuler,
and
R.Seckler
(1998).
Phage P22 tailspike protein: removal of head-binding domain unmasks effects of folding mutations on native-state thermal stability.
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Protein Sci,
7,
2223-2232.
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S.Steinbacher,
S.Miller,
U.Baxa,
A.Weintraub,
and
R.Seckler
(1997).
Interaction of Salmonella phage P22 with its O-antigen receptor studied by X-ray crystallography.
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Biol Chem,
378,
337-343.
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W.I.Weis
(1997).
Cell-surface carbohydrate recognition by animal and viral lectins.
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Curr Opin Struct Biol,
7,
624-630.
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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
codes are
shown on the right.
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