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PDBsum entry 2w20

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
2w20
Jmol
Contents
Protein chains
470 a.a. *
Ligands
MES ×2
GOL ×3
Metals
_CL ×3
Waters ×1025
* Residue conservation analysis
PDB id:
2w20
Name: Hydrolase
Title: Structure of the catalytic domain of the native nana sialidase from streptococcus pneumoniae
Structure: Sialidase a. Chain: a, b. Fragment: catalytic domain, residues 321-791. Synonym: neuraminidase a, nana sialidase. Engineered: yes
Source: Streptococcus pneumoniae. Organism_taxid: 171101. Strain: r6. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.49Å     R-factor:   0.201     R-free:   0.225
Authors: G.Xu,P.W.Andrew,G.L.Taylor
Key ref: G.Xu et al. (2008). Structure of the catalytic domain of Streptococcus pneumoniae sialidase NanA. Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 772-775. PubMed id: 18765901
Date:
21-Oct-08     Release date:   23-Dec-08    
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.
470 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  

 

 
Acta Crystallogr Sect F Struct Biol Cryst Commun 64:772-775 (2008)
PubMed id: 18765901  
 
 
Structure of the catalytic domain of Streptococcus pneumoniae sialidase NanA.
G.Xu, X.Li, P.W.Andrew, G.L.Taylor.
 
  ABSTRACT  
 
Streptococcus pneumoniae genomes encode three sialidases, NanA, NanB and NanC, which are key virulence factors that remove sialic acids from various glycoconjugates. The enzymes have potential as drug targets and also as vaccine candidates. The 115 kDa NanA is the largest of the three sialidases and is anchored to the bacterial membrane. Although recombinantly expressed full-length NanA was soluble, it failed to crystallize; therefore, a 56.5 kDa domain that retained full enzyme activity was subcloned. The purified enzyme was crystallized in 0.1 M MES pH 6.5, 30%(w/v) PEG 4000 using the sitting-drop vapour-diffusion method. Data were collected at 100 K to 2.5 A resolution from a crystal grown in the presence of the inhibitor 2-deoxy-2,3-dehydro-N-acetyl neuraminic acid. The crystal belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 49.2, b = 95.6, c = 226.6 A. The structure was solved by molecular replacement and refined to final R and R(free) factors of 0.246 and 0.298, respectively.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21314964 E.M.Vilei, A.Johansson, Y.Schlatter, K.Redhead, and J.Frey (2011).
Genetic and functional characterization of the NanA sialidase from Clostridium chauvoei.
  Vet Res, 42, 2.  
19594936 E.M.Quistgaard, and S.S.Thirup (2009).
Sequence and structural analysis of the Asp-box motif and Asp-box beta-propellers; a widespread propeller-type characteristic of the Vps10 domain family and several glycoside hydrolase families.
  BMC Struct Biol, 9, 46.  
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