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PDBsum entry 2yfo

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protein ligands metals links
Hydrolase PDB id
2yfo
Jmol
Contents
Protein chain
719 a.a.
Ligands
GOL
PGE ×4
PO4
GLA
GAL
Metals
_NA ×27
Waters ×1071
PDB id:
2yfo
Name: Hydrolase
Title: Galactosidase domain of alpha-galactosidase-sucrose kinase, agask, in complex with galactose
Structure: Alpha-galactosidase-sucrose kinase agask. Chain: a. Engineered: yes
Source: Ruminococcus gnavus e1. Organism_taxid: 935582. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.35Å     R-factor:   0.125     R-free:   0.141
Authors: G.Sulzenbacher,L.Bruel,M.Tison-Cervera,A.Pujol,C.Nicoletti,J A.Galinier,D.Ropartz,M.Fons,F.Pompeo,T.Giardina
Key ref: L.Bruel et al. (2011). α-Galactosidase/sucrose kinase (AgaSK), a novel bifunctional enzyme from the human microbiome coupling galactosidase and kinase activities. J Biol Chem, 286, 40814-40823. PubMed id: 21931163 DOI: 10.1074/jbc.M111.286039
Date:
07-Apr-11     Release date:   28-Sep-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
G3XAP8  (G3XAP8_RUMGN) -  Alpha-galactosidase-sucrose kinase agask
Seq:
Struc:
 
Seq:
Struc:
720 a.a.
719 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.22  - Alpha-galactosidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Melibiose + H2O = galactose + glucose

+
=
+
      Cofactor: Mg(2+); NAD(+)
Mg(2+)
NAD(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     carbohydrate metabolic process   1 term 
  Biochemical function     catalytic activity     5 terms  

 

 
    reference    
 
 
DOI no: 10.1074/jbc.M111.286039 J Biol Chem 286:40814-40823 (2011)
PubMed id: 21931163  
 
 
α-Galactosidase/sucrose kinase (AgaSK), a novel bifunctional enzyme from the human microbiome coupling galactosidase and kinase activities.
L.Bruel, G.Sulzenbacher, M.Cervera Tison, A.Pujol, C.Nicoletti, J.Perrier, A.Galinier, D.Ropartz, M.Fons, F.Pompeo, T.Giardina.
 
  ABSTRACT  
 
α-Galactosides are non-digestible carbohydrates widely distributed in plants. They are a potential source of energy in our daily food, and their assimilation by microbiota may play a role in obesity. In the intestinal tract, they are degraded by microbial glycosidases, which are often modular enzymes with catalytic domains linked to carbohydrate-binding modules. Here we introduce a bifunctional enzyme from the human intestinal bacterium Ruminococcus gnavus E1, α-galactosidase/sucrose kinase (AgaSK). Sequence analysis showed that AgaSK is composed of two domains: one closely related to α-galactosidases from glycoside hydrolase family GH36 and the other containing a nucleotide-binding motif. Its biochemical characterization showed that AgaSK is able to hydrolyze melibiose and raffinose to galactose and either glucose or sucrose, respectively, and to specifically phosphorylate sucrose on the C6 position of glucose in the presence of ATP. The production of sucrose-6-P directly from raffinose points toward a glycolytic pathway in bacteria, not described so far. The crystal structures of the galactosidase domain in the apo form and in complex with the product shed light onto the reaction and substrate recognition mechanisms and highlight an oligomeric state necessary for efficient substrate binding and suggesting a cross-talk between the galactose and kinase domains.