PDBsum entry 2v5i

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protein metals links
Viral protein PDB id
Protein chain
553 a.a.
Waters ×831
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
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. (2008). Structure of the receptor-binding protein of bacteriophage det7: a podoviral tail spike in a myovirus. J Virol, 82, 2265-2273. PubMed id: 18077713
05-Jul-07     Release date:   19-Feb-08    
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Protein chain
No UniProt id for this chain
Struc: 553 a.a.
Key:    Secondary structure  CATH domain


J Virol 82:2265-2273 (2008)
PubMed id: 18077713  
Structure of the receptor-binding protein of bacteriophage det7: a podoviral tail spike 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.
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 tail spike 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 tail spikes attached to a very short, noncontractile tail. The amino-terminal 150 residues of the Det7 protein lack homology to the P22 tail spike and are probably responsible for binding to the base plate of the myoviral tail. Det7 tail spike lacking this putative particle-binding domain was purified from Escherichia coli, and well-diffracting crystals of the protein were obtained. The structure, determined by molecular replacement and refined at a 1.6-A resolution, is very similar to that of bacteriophage P22 tail spike. Fluorescence titrations with an octasaccharide suggest Det7 tail spike to bind its receptor lipopolysaccharide somewhat less tightly than the P22 tail spike. The Det7 tail spike 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, the Det7 tail spike lacks both carboxy-terminal cysteines previously proposed to form a transient disulfide during P22 tail spike 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
21330133 E.C.Schulz, and R.Ficner (2011).
Knitting and snipping: chaperones in β-helix folding.
  Curr Opin Struct Biol, 21, 232-239.  
21124920 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.  
19349519 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.  
19631658 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: 3hon 3hsh
18433454 P.G.Leiman, and I.J.Molineux (2008).
Evolution of a new enzyme activity from the same motif fold.
  Mol Microbiol, 69, 287-290.  
18550341 S.R.Casjens (2008).
Diversity among the tailed-bacteriophages that infect the Enterobacteriaceae.
  Res Microbiol, 159, 340-348.  
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