 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Viral protein
|
PDB id
|
|
|
|
2v5i
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Viral protein
|
|
|
Title:
|
|
Structure of the receptor-binding protein of bacteriophage det7: a podoviral tailspike in a myovirus
|
|
Structure:
|
|
Salmonella typhimurium db7155 bacteriophage det7 tailspike. Chain: a. Fragment: o-antigen binding and hydrolysis domain and c- terminal intertwined domain, residues 150-708. Engineered: yes
|
|
Source:
|
|
Bacteriophage. Organism_taxid: 38018. Strain: det7. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_variant: de3. Other_details: regensburg sewage, germany
|
|
Resolution:
|
|
|
1.60Å
|
R-factor:
|
0.142
|
R-free:
|
0.170
|
|
|
Authors:
|
|
M.Walter,C.Fiedler,R.Grassl,M.Biebl,R.Rachel, X.L.Hermo-Parrado,A.L.Llamas-Saiz,R.Seckler,S.Miller, M.J.Van Raaij
|
|
Key ref:
|
|
M.Walter
et al.
(2007).
Structure of the receptor-binding protein of bacteriophage Det7: A podoviral tailspike in a myovirus.
J Virol,
82,
2265.
PubMed id:
DOI:
|
|
|
Date:
|
|
|
05-Jul-07
|
Release date:
|
19-Feb-08
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
DOI no:
|
J Virol
82:2265
(2007)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Structure of the receptor-binding protein of bacteriophage Det7: A podoviral tailspike in a myovirus.
|
|
M.Walter,
C.Fiedler,
R.Grassl,
M.Biebl,
R.Rachel,
X.L.Hermo-Parrado,
A.L.Llamas-Saiz,
R.Seckler,
S.Miller,
M.J.van Raaij.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
A new Salmonella enterica phage, Det7, was isolated from sewage and shown by
electron microscopy to belong to the myoviridae morphogroup of bacteriophages.
Det7 contains a 75 kDa protein with 50 % overall sequence identity to the
tailspike endorhamnosidase of podovirus P22. Adsorption of myoviruses to their
bacterial hosts is normally mediated by long and short tail fibers attached to a
contractile tail, whereas podoviruses do not contain fibers, but attach to host
cells through stubby tailspikes attached to a very short, non-contractile tail.
The amino-terminal 150 residues of the Det7 protein lack homology to the P22
tailspike and are probably responsible for binding to the base plate of the
myoviral tail. Det7 tailspike lacking this putative particle-binding domain was
purified from E. coli and well-diffracting crystals of the protein were
obtained. The structure, solved by molecular replacement and refined at 1.6 A
resolution, is very similar to that of bacteriophage P22 tailspike. Fluorescence
titrations with an octasaccharide suggest Det7 tailspike to bind its receptor
lipopolysaccharide somewhat less tightly than the P22 tailspike. The Det7
tailspike is even more resistant to thermal unfolding than the already
exceptionally stable homologue from P22. Folding and assembly of both trimeric
proteins are equally temperature-sensitive and equally slow. Despite the close
structural, biochemical, and sequence similarities between both proteins, Det7
tailspike lacks both carboxy-terminal cysteines previously proposed to form a
transient disulfide during P22 tailspike assembly. Our data suggest
receptor-binding module exchange between podoviruses and myoviruses in the
course of bacteriophage evolution.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
|
| |
PubMed id
|
|
Reference
|
|
|
|
|
|
E.C.Schulz,
and
R.Ficner
(2011).
Knitting and snipping: chaperones in β-helix folding.
|
| |
Curr Opin Struct Biol, 21,
232-239.
|
|
|
|
|
|
|
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.
|
| |
PLoS One, 5,
e13904.
|
|
|
|
|
|
|
D.Scholl,
M.Cooley,
S.R.Williams,
D.Gebhart,
D.Martin,
A.Bates,
and
R.Mandrell
(2009).
An engineered R-type pyocin is a highly specific and sensitive bactericidal agent for the food-borne pathogen Escherichia coli O157:H7.
|
| |
Antimicrob Agents Chemother, 53,
3074-3080.
|
|
|
|
|
|
|
S.P.Boudko,
T.Sasaki,
J.Engel,
T.F.Lerch,
J.Nix,
M.S.Chapman,
and
H.P.Bächinger
(2009).
Crystal structure of human collagen XVIII trimerization domain: A novel collagen trimerization Fold.
|
| |
J Mol Biol, 392,
787-802.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
P.G.Leiman,
and
I.J.Molineux
(2008).
Evolution of a new enzyme activity from the same motif fold.
|
| |
Mol Microbiol, 69,
287-290.
|
|
|
|
|
|
|
S.R.Casjens
(2008).
Diversity among the tailed-bacteriophages that infect the Enterobacteriaceae.
|
| |
Res Microbiol, 159,
340-348.
|
|
|
|
|
|
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.
|
Links
