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PDBsum entry 3h71

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protein Protein-protein interface(s) links
Hydrolase PDB id
3h71
Jmol
Contents
Protein chains
474 a.a. *
Waters ×1745
* Residue conservation analysis
PDB id:
3h71
Name: Hydrolase
Title: Crystal structure of streptococcus pneumoniae d39 neuraminidase a precursor (nana)
Structure: Sialidase a. Chain: a, b. Fragment: unp residues 317-793. Synonym: neuraminidase a. Engineered: yes
Source: Streptococcus pneumoniae. Organism_taxid: 171101. Strain: r6. Gene: nana, spr1536. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.70Å     R-factor:   0.172     R-free:   0.198
Authors: Y.-S.Hsiao,L.Tong
Key ref: Y.S.Hsiao et al. (2009). Crystal structures of respiratory pathogen neuraminidases. Biochem Biophys Res Commun, 380, 467-471. PubMed id: 19284989 DOI: 10.1016/j.bbrc.2009.01.108
Date:
24-Apr-09     Release date:   12-May-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P62576  (NANA_STRR6) -  Sialidase A
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1035 a.a.
474 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.18  - Exo-alpha-sialidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)-glycosidic linkages of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     pathogenesis   1 term 
  Biochemical function     exo-alpha-sialidase activity     1 term  

 

 
DOI no: 10.1016/j.bbrc.2009.01.108 Biochem Biophys Res Commun 380:467-471 (2009)
PubMed id: 19284989  
 
 
Crystal structures of respiratory pathogen neuraminidases.
Y.S.Hsiao, D.Parker, A.J.Ratner, A.Prince, L.Tong.
 
  ABSTRACT  
 
Currently there is pressing need to develop novel therapeutic agents for the treatment of infections by the human respiratory pathogens Pseudomonas aeruginosa and Streptococcus pneumoniae. The neuraminidases of these pathogens are important for host colonization in animal models of infection and are attractive targets for drug discovery. To aid in the development of inhibitors against these neuraminidases, we have determined the crystal structures of the P. aeruginosa enzyme NanPs and S. pneumoniae enzyme NanA at 1.6 and 1.7A resolution, respectively. In situ proteolysis with trypsin was essential for the crystallization of our recombinant NanA. The active site regions of the two enzymes are strikingly different. NanA contains a deep pocket that is similar to that in canonical neuraminidases, while the NanPs active site is much more open. The comparative studies suggest that NanPs may not be a classical neuraminidase, and may have distinct natural substrates and physiological functions. This work represents an important step in the development of drugs to prevent respiratory tract colonization by these two pathogens.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20557315 A.Banerjee, N.M.Van Sorge, T.R.Sheen, S.Uchiyama, T.J.Mitchell, and K.S.Doran (2010).
Activation of brain endothelium by pneumococcal neuraminidase NanA promotes bacterial internalization.
  Cell Microbiol, 12, 1576-1588.  
19564377 D.Parker, G.Soong, P.Planet, J.Brower, A.J.Ratner, and A.Prince (2009).
The NanA neuraminidase of Streptococcus pneumoniae is involved in biofilm formation.
  Infect Immun, 77, 3722-3730.  
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.