spacer
spacer

PDBsum entry 1j0y

Go to PDB code: 
protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
1j0y
Jmol
Contents
Protein chains
516 a.a. *
Ligands
BGC ×4
Metals
_CA ×4
Waters ×635
* Residue conservation analysis
PDB id:
1j0y
Name: Hydrolase
Title: Beta-amylase from bacillus cereus var. Mycoides in complex with glucose
Structure: Beta-amylase. Chain: a, b, c, d. Synonym: 1,4-alpha-d-glucan maltohydrolase. Ec: 3.2.1.2
Source: Bacillus cereus. Organism_taxid: 1396. Strain: var. Mycoides
Resolution:
2.10Å     R-factor:   0.179     R-free:   0.236
Authors: T.Oyama,H.Miyake,M.Kusunoki,Y.Nitta
Key ref: T.Oyama et al. (2003). Crystal structures of beta-amylase from Bacillus cereus var mycoides in complexes with substrate analogs and affinity-labeling reagents. J Biochem, 133, 467-474. PubMed id: 12761294
Date:
25-Nov-02     Release date:   17-Jun-03    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P36924  (AMYB_BACCE) -  Beta-amylase
Seq:
Struc:
 
Seq:
Struc:
546 a.a.
516 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.2  - Beta-amylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of 1,4-alpha-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   4 terms 
  Biochemical function     starch binding     5 terms  

 

 
J Biochem 133:467-474 (2003)
PubMed id: 12761294  
 
 
Crystal structures of beta-amylase from Bacillus cereus var mycoides in complexes with substrate analogs and affinity-labeling reagents.
T.Oyama, H.Miyake, M.Kusunoki, Y.Nitta.
 
  ABSTRACT  
 
The crystal structures of beta-amylase from Bacillus cereus var. mycoides in complexes with five inhibitors were solved. The inhibitors used were three substrate analogs, i.e. glucose, maltose (product), and a synthesized compound, O-alpha-D-glucopyranosyl-(1-->4)-O-alpha-D-glucopyranosyl-(1-->4)-D-xylopyranose (GGX), and two affinity-labeling reagents with an epoxy alkyl group at the reducing end of glucose. For all inhibitors, one molecule was bound at the active site cleft and the non-reducing end glucose of the four inhibitors except GGX was located at subsite 1, accompanied by a large conformational change of the flexible loop (residues 93-97), which covered the bound inhibitor. In addition, another molecule of maltose or GGX was bound about 30 A away from the active site. A large movement of residues 330 and 331 around subsite 3 was also observed upon the binding of GGX at subsites 3 to 5. Two affinity-labeling reagents, alpha-EPG and alpha-EBG, were covalently bound to a catalytic residue (Glu-172). A substrate recognition mechanism for the beta-amylase was discussed based on the modes of binding of these inhibitors in the active site cleft.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19682075 C.Christiansen, M.Abou Hachem, S.Janecek, A.Viksø-Nielsen, A.Blennow, and B.Svensson (2009).
The carbohydrate-binding module family 20--diversity, structure, and function.
  FEBS J, 276, 5006-5029.  
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.