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PDBsum entry 3gvl

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protein ligands links
Hydrolase PDB id
3gvl
Jmol
Contents
Protein chain
670 a.a. *
Ligands
SLB
SLB-SIA
Waters ×1401
* Residue conservation analysis
PDB id:
3gvl
Name: Hydrolase
Title: Crystal structure of endo-neuraminidasenf
Structure: Endo-n-acetylneuraminidase. Chain: a. Fragment: residues 246-910. Synonym: endo-alpha-sialidase, gp17 protein. Engineered: yes
Source: Enterobacteria phage k1f. Bacteriophage k1f. Organism_taxid: 344021. Gene: sia, 17, 17.0. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.41Å     R-factor:   0.169     R-free:   0.188
Authors: E.C.Schulz,A.Dickmanns,R.Ficner
Key ref: E.C.Schulz et al. (2010). Structural basis for the recognition and cleavage of polysialic acid by the bacteriophage K1F tailspike protein EndoNF. J Mol Biol, 397, 341-351. PubMed id: 20096705 DOI: 10.1016/j.jmb.2010.01.028
Date:
31-Mar-09     Release date:   02-Mar-10    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q04830  (ENAN_BPK1F) -  Endo-N-acetylneuraminidase
Seq:
Struc:
 
Seq:
Struc:
920 a.a.
670 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.129  - Endo-alpha-sialidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Endohydrolysis of (2->8)-alpha-sialosyl linkages in oligo- or poly(sialic) acids.

 

 
DOI no: 10.1016/j.jmb.2010.01.028 J Mol Biol 397:341-351 (2010)
PubMed id: 20096705  
 
 
Structural basis for the recognition and cleavage of polysialic acid by the bacteriophage K1F tailspike protein EndoNF.
E.C.Schulz, D.Schwarzer, M.Frank, K.Stummeyer, M.Mühlenhoff, A.Dickmanns, R.Gerardy-Schahn, R.Ficner.
 
  ABSTRACT  
 
An alpha-2,8-linked polysialic acid (polySia) capsule confers immune tolerance to neuroinvasive, pathogenic prokaryotes such as Escherichia coli K1 and Neisseria meningitidis and supports host infection by means of molecular mimicry. Bacteriophages of the K1 family, infecting E. coli K1, specifically recognize and degrade this polySia capsule utilizing tailspike endosialidases. While the crystal structure for the catalytic domain of the endosialidase of bacteriophage K1F (endoNF) has been solved, there is yet no structural information on the mode of polySia binding and cleavage available. The crystal structure of activity deficient active-site mutants of the homotrimeric endoNF cocrystallized with oligomeric sialic acid identified three independent polySia binding sites in each endoNF monomer. The bound oligomeric sialic acid displays distinct conformations at each site. In the active site, a Sia(3) molecule is bound in an extended conformation representing the enzyme-product complex. Structural and biochemical data supported by molecular modeling enable to propose a reaction mechanism for polySia cleavage by endoNF.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
  20875143 Y.Chai, H.Xiong, X.Ma, L.Cheng, G.Huang, and Z.R.Zhang (2010).
Molecular characterization, structural analysis and determination of host range of a novel bacteriophage LSB-1.
  Virol J, 7, 255.  
20602419 Y.Su, C.Kasper, A.Kirschning, G.Dräger, and S.Berski (2010).
Synthesis of new polysialic acid derivatives.
  Macromol Biosci, 10, 1028-1033.  
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