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PDBsum entry 2zox

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protein ligands metals links
Hydrolase PDB id
2zox
Jmol
Contents
Protein chain
466 a.a. *
Ligands
GLC
PNG
PO4
PLM ×2
OLA
GOL
Metals
_MG ×2
Waters ×196
* Residue conservation analysis
PDB id:
2zox
Name: Hydrolase
Title: Crystal structure of the covalent intermediate of human cyto beta-glucosidase
Structure: Cytosolic beta-glucosidase. Chain: a. Synonym: cytosolic beta-glucosidase-like protein 1. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gba3, cbg, cbgl1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.90Å     R-factor:   0.192     R-free:   0.226
Authors: J.Noguchi,Y.Hayashi,Y.Baba,N.Okino,M.Kimura,M.Ito,Y.Kakuta
Key ref: J.Noguchi et al. (2008). Crystal structure of the covalent intermediate of human cytosolic beta-glucosidase. Biochem Biophys Res Commun, 374, 549-552. PubMed id: 18662675 DOI: 10.1016/j.bbrc.2008.07.089
Date:
17-Jun-08     Release date:   30-Sep-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9H227  (GBA3_HUMAN) -  Cytosolic beta-glucosidase
Seq:
Struc:
469 a.a.
466 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.21  - Beta-glucosidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   2 terms 
  Biological process     metabolic process   7 terms 
  Biochemical function     hydrolase activity     6 terms  

 

 
DOI no: 10.1016/j.bbrc.2008.07.089 Biochem Biophys Res Commun 374:549-552 (2008)
PubMed id: 18662675  
 
 
Crystal structure of the covalent intermediate of human cytosolic beta-glucosidase.
J.Noguchi, Y.Hayashi, Y.Baba, N.Okino, M.Kimura, M.Ito, Y.Kakuta.
 
  ABSTRACT  
 
Human cytosolic beta-glucosidase, also known as klotho-related protein (KLrP, GBA3), is an enzyme that hydrolyzes various beta-D-glucosides, including glucosylceramide. We recently reported the crystal structure of KLrP in complex with glucose [Y. Hayashi, N. Okino, Y. Kakuta, T. Shikanai, M. Tani, H. Narimatsu, M. Ito, Klotho-related protein is a novel cytosolic neutral beta-glycosylceramidase, J. Biol. Chem. 282 (2007) 30889-30900]. Here, we report the crystal structure of a covalent intermediate of the KLrP mutant E165Q, in which glucose was covalently bound to a nucleophile, Glu(373). The structure confirms the double displacement mechanism of the retaining beta-glucosidase. In addition, the structure suggests that a water molecule could be involved in the stabilization of transition states through a sugar, 2-hydroxyl.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20490603 J.R.Ketudat Cairns, and A.Esen (2010).
β-Glucosidases.
  Cell Mol Life Sci, 67, 3389-3405.  
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.