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PDBsum entry 3a75

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protein ligands Protein-protein interface(s) links
Transferase PDB id
3a75
Jmol
Contents
Protein chains
359 a.a. *
182 a.a. *
Ligands
GLU ×2
Waters ×790
* Residue conservation analysis
PDB id:
3a75
Name: Transferase
Title: Crystal structure of glutamate complex of halotolerant γ-glutamyltranspeptidase from bacillus subtilis
Structure: Gamma-glutamyltranspeptidase large chain. Chain: a, c. Engineered: yes. Gamma-glutamyltranspeptidase small chain. Chain: b, d. Engineered: yes
Source: Bacillus subtilis. Organism_taxid: 1423. Strain: 168. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.95Å     R-factor:   0.208     R-free:   0.262
Authors: K.Wada,K.Fukuyama
Key ref: K.Wada et al. (2010). Crystal structure of the halotolerant gamma-glutamyltranspeptidase from Bacillus subtilis in complex with glutamate reveals a unique architecture of the solvent-exposed catalytic pocket. FEBS J, 277, 1000-1009. PubMed id: 20088880
Date:
14-Sep-09     Release date:   09-Mar-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P54422  (GGT_BACSU) -  Gamma-glutamyltranspeptidase
Seq:
Struc:
 
Seq:
Struc:
587 a.a.
359 a.a.
Protein chains
Pfam   ArchSchema ?
P54422  (GGT_BACSU) -  Gamma-glutamyltranspeptidase
Seq:
Struc:
 
Seq:
Struc:
587 a.a.
182 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class 2: Chains A, B, C, D: E.C.2.3.2.2  - Gamma-glutamyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: A (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
(5-L-glutamyl)-peptide
+ amino acid
= peptide
+
5-L-glutamyl amino acid
Bound ligand (Het Group name = GLU)
matches with 56.00% similarity
   Enzyme class 3: Chains A, B, C, D: E.C.3.4.19.13  - Glutathione hydrolase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Glutathione + H2O = L-cysteinylglycine + L-glutamate
Glutathione
+ H(2)O
= L-cysteinylglycine
+ L-glutamate
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     glutathione metabolic process   1 term 
  Biochemical function     gamma-glutamyltransferase activity     1 term  

 

 
    reference    
 
 
FEBS J 277:1000-1009 (2010)
PubMed id: 20088880  
 
 
Crystal structure of the halotolerant gamma-glutamyltranspeptidase from Bacillus subtilis in complex with glutamate reveals a unique architecture of the solvent-exposed catalytic pocket.
K.Wada, M.Irie, H.Suzuki, K.Fukuyama.
 
  ABSTRACT  
 
gamma-Glutamyltranspeptidase (GGT; EC 2.3.2.2), an enzyme found in organisms from bacteria to mammals and plants, plays a central role in glutathione metabolism. Structural studies of GGTs from Escherichia coli and Helicobacter pylori have revealed detailed molecular mechanisms of catalysis and maturation. In these two GGTs, highly conserved residues form the catalytic pockets, conferring the ability of the loop segment to shield the bound gamma-glutamyl moiety from the solvent. Here, we have examined the Bacillus subtilis GGT, which apparently lacks the amino acids corresponding to the lid-loop that are present in mammalian and plant GGTs as well as in most bacterial GGTs. Another remarkable feature of B. subtilis GGT is its salt tolerance; it retains 86% of its activity even in 3 m NaCl. To better understand these characteristics of B. subtilis GGT, we determined its crystal structure in complex with glutamate, a product of the enzymatic reaction, at 1.95 A resolution. This structure revealed that, unlike the E. coli and H. pylori GGTs, the catalytic pocket of B. subtilis GGT has no segment that covers the bound glutamate; consequently, the glutamate is exposed to solvent. Furthermore, calculation of the electrostatic potential showed that strong acidic patches were distributed on the surface of the B. subtilis GGT, even under high-salt conditions, and this may allow the protein to remain in the hydrated state and avoid self-aggregation. The structural findings presented here have implications for the molecular mechanism of GGT.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21298394 I.Castellano, A.Di Salle, A.Merlino, M.Rossi, and F.La Cara (2011).
Gene cloning and protein expression of γ-glutamyltranspeptidases from Thermus thermophilus and Deinococcus radiodurans: comparison of molecular and structural properties with mesophilic counterparts.
  Extremophiles, 15, 259-270.  
20572278 H.Suzuki, C.Yamada, K.Kijima, S.Ishihara, K.Wada, K.Fukuyama, and H.Kumagai (2010).
Enhancement of glutaryl-7-aminocephalosporanic acid acylase activity of gamma-glutamyltranspeptidase of Bacillus subtilis.
  Biotechnol J, 5, 829-837.  
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.