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PDBsum entry 3fax

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protein ligands metals links
Hydrolase PDB id
3fax
Jmol
Contents
Protein chain
771 a.a. *
Ligands
BGC-GLC-GLC
Metals
_CL
_CA ×4
Waters ×63
* Residue conservation analysis
PDB id:
3fax
Name: Hydrolase
Title: The crystal structure of gbs pullulanase sap in complex with maltotetraose
Structure: Reticulocyte binding protein. Chain: a. Fragment: n2, n3, a and c pullulanase domains, unp residues engineered: yes
Source: Streptococcus agalactiae coh1. Organism_taxid: 342616. Gene: san_1346. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.40Å     R-factor:   0.224     R-free:   0.283
Authors: L.J.Gourlay
Key ref: L.J.Gourlay et al. (2009). Group B streptococcus pullulanase crystal structures in the context of a novel strategy for vaccine development. J Bacteriol, 191, 3544-3552. PubMed id: 19329633
Date:
18-Nov-08     Release date:   14-Apr-09    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q3DB05  (Q3DB05_STRAG) -  Reticulocyte binding protein
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1252 a.a.
771 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     carbohydrate metabolic process   1 term 
  Biochemical function     catalytic activity     3 terms  

 

 
J Bacteriol 191:3544-3552 (2009)
PubMed id: 19329633  
 
 
Group B streptococcus pullulanase crystal structures in the context of a novel strategy for vaccine development.
L.J.Gourlay, I.Santi, A.Pezzicoli, G.Grandi, M.Soriani, M.Bolognesi.
 
  ABSTRACT  
 
The group B streptococcus type I pullulanase (SAP) is a class 13 glycoside hydrolase that is anchored to the bacterial cell surface via a conserved C-terminal anchoring motif and involved in alpha-glucan degradation. Recent in vitro functional studies have shown that SAP is immunogenic in humans and that anti-SAP sera derived from immunized animals impair both group A and group B streptococcus pullulanase activities, suggesting that in vivo immunization with this antigen could prevent streptococcal colonization. To further investigate the putative role of SAP in bacterial pathogenesis, we carried out functional studies and found that recombinant SAP binds to human cervical epithelial cells. Furthermore, with a view of using SAP as a vaccine candidate, we present high-resolution crystal structure analyses of an N-terminally truncated form of SAP lacking the carbohydrate binding module but containing the catalytic domain and displaying glycosidase hydrolase activity, both in its apo form and in complex with maltotetraose, at resolutions of 2.1 and 2.4 A, respectively.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20522493 M.L.Ferrando, S.Fuentes, A.de Greeff, H.Smith, and J.M.Wells (2010).
ApuA, a multifunctional alpha-glucan-degrading enzyme of Streptococcus suis, mediates adhesion to porcine epithelium and mucus.
  Microbiology, 156, 2818-2828.  
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