PDBsum entry 2vji

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Viral protein PDB id
Protein chain
598 a.a.
Waters ×935
PDB id:
Name: Viral protein
Title: Tailspike protein of e.Coli bacteriophage hk620
Structure: Tailspike protein. Chain: a. Fragment: lacking the n-terminal head-binding domain, residues 111-710. Synonym: hk620 tailspike protein. Engineered: yes
Source: Bacteriophage hk620. Organism_taxid: 155148. Strain: h. Expressed in: escherichia coli. Expression_system_taxid: 469008.
1.38Å     R-factor:   0.151     R-free:   0.180
Authors: J.J.Mueller,S.Barbirz,C.Uetrecht,R.Seckler,U.Heinemann
Key ref: S.Barbirz et al. (2008). Crystal structure of Escherichia coli phage HK620 tailspike: podoviral tailspike endoglycosidase modules are evolutionarily related. Mol Microbiol, 69, 303-316. PubMed id: 18547389
11-Dec-07     Release date:   01-Jul-08    
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Protein chain
Pfam   ArchSchema ?
Q9AYY6  (Q9AYY6_BPHK6) -  Tail spike protein
710 a.a.
598 a.a.
Key:    PfamA domain  Secondary structure  CATH domain


Mol Microbiol 69:303-316 (2008)
PubMed id: 18547389  
Crystal structure of Escherichia coli phage HK620 tailspike: podoviral tailspike endoglycosidase modules are evolutionarily related.
S.Barbirz, J.J.Müller, C.Uetrecht, A.J.Clark, U.Heinemann, R.Seckler.
Bacteriophage HK620 infects Escherichia coli H and is closely related to Shigella phage Sf6 and Salmonella phage P22. All three Podoviridae recognize and cleave their respective host cell receptor polysaccharide by homotrimeric tailspike proteins. The three proteins exhibit high sequence identity in the 110 residues of their N-terminal particle-binding domains, but no apparent sequence similarity in their major, receptor-binding parts. We have biochemically characterized the receptor-binding part of HK620 tailspike and determined its crystal structure to 1.38 A resolution. Its major domain is a right-handed parallel beta-helix, as in Sf6 and P22 tailspikes. HK620 tailspike has endo-N-acetylglucosaminidase activity and produces hexasaccharides of an O18A1-type O-antigen. As indicated by the structure of a hexasaccharide complex determined at 1.6 A resolution, the endoglycosidase-active sites are located intramolecularly, as in P22, and not between subunits, as in Sf6 tailspike. In contrast, the extreme C-terminal domain of HK620 tailspike forms a beta-sandwich, as in Sf6 and unlike P22 tailspike. Despite the different folds, structure-based sequence alignments of the C-termini reveal motifs conserved between the three proteins. We propose that the tailspike genes of P22, Sf6 and HK620 have a common precursor and are not mosaics of unrelated gene fragments.

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.  
20118935 E.C.Schulz, A.Dickmanns, H.Urlaub, A.Schmitt, M.Mühlenhoff, K.Stummeyer, D.Schwarzer, R.Gerardy-Schahn, and R.Ficner (2010).
Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding.
  Nat Struct Mol Biol, 17, 210-215.
PDB codes: 3gud 3gw6
20006993 J.J.Bull, E.R.Vimr, and I.J.Molineux (2010).
A tale of tails: Sialidase is key to success in a model of phage therapy against K1-capsulated Escherichia coli.
  Virology, 398, 79-86.  
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.  
19189967 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.
  J Biol Chem, 284, 9465-9474.  
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.  
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