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PDBsum entry 3ih9

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protein Protein-protein interface(s) links
Hydrolase PDB id
3ih9
Jmol
Contents
Protein chains
448 a.a. *
Waters ×288
* Residue conservation analysis
PDB id:
3ih9
Name: Hydrolase
Title: Crystal structure analysis of mglu in its tris form
Structure: Salt-tolerant glutaminase. Chain: a, b. Engineered: yes
Source: Micrococcus luteus. Micrococcus lysodeikticus. Organism_taxid: 1270. Strain: k-3. Gene: glutaminase. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.50Å     R-factor:   0.217     R-free:   0.258
Authors: K.Yoshimune,Y.Shirakihara
Key ref: K.Yoshimune et al. (2010). Crystal structure of salt-tolerant glutaminase from Micrococcus luteus K-3 in the presence and absence of its product L-glutamate and its activator Tris. FEBS J, 277, 738-748. PubMed id: 20050917
Date:
29-Jul-09     Release date:   19-Jan-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q4U1A6  (Q4U1A6_MICLU) -  Glutaminase
Seq:
Struc:
456 a.a.
448 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.5.1.2  - Glutaminase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-glutamine + H2O = L-glutamate + NH3
L-glutamine
+ H(2)O
= L-glutamate
+ NH(3)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     glutamine metabolic process   1 term 
  Biochemical function     hydrolase activity     2 terms  

 

 
    Added reference    
 
 
FEBS J 277:738-748 (2010)
PubMed id: 20050917  
 
 
Crystal structure of salt-tolerant glutaminase from Micrococcus luteus K-3 in the presence and absence of its product L-glutamate and its activator Tris.
K.Yoshimune, Y.Shirakihara, M.Wakayama, I.Yumoto.
 
  ABSTRACT  
 
Glutaminase from Micrococcus luteus K-3 [Micrococcus glutaminase (Mglu); 456 amino acid residues (aa); 48 kDa] is a salt-tolerant enzyme. Our previous study determined the structure of its major 42-kDa fragment. Here, using new crystallization conditions, we determined the structures of the intact enzyme in the presence and absence of its product L-glutamate and its activator Tris, which activates the enzyme by sixfold. With the exception of a 'lid' part (26-29 aa) and a few other short stretches, the structures were all very similar over the entire polypeptide chain. However, the presence of the ligands significantly reduced the length of the disordered regions: 41 aa in the unliganded structure (N), 21 aa for L-glutamate (G), 8 aa for Tris (T) and 6 aa for both L-glutamate and Tris (TG). L-glutamate was identified in both the G and TG structures, whereas Tris was only identified in the TG structure. Comparison of the glutamate-binding site between Mglu and salt-labile glutaminase (YbgJ) from Bacillus subtilis showed significantly smaller structural changes of the protein part in Mglu. A comparison of the substrate-binding pocket of Mglu, which is highly specific for L-glutamine, with that of Erwinia carotovora asparaginase, which has substrates other than L-glutamine, shows that Mglu has a larger substrate-binding pocket that prevents the binding of L-asparagine with proper interactions.