spacer
spacer

PDBsum entry 1jlw

Go to PDB code: 
protein Protein-protein interface(s) links
Transferase PDB id
1jlw
Jmol
Contents
Protein chains
217 a.a. *
Waters ×40
* Residue conservation analysis
PDB id:
1jlw
Name: Transferase
Title: Anopheles dirus species b glutathione s-transferases 1-4
Structure: Glutathione transferase gst1-4. Chain: a, b. Engineered: yes
Source: Anopheles cracens. Organism_taxid: 123217. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Dimer (from PQS)
Resolution:
2.45Å     R-factor:   0.223     R-free:   0.271
Authors: A.J.Oakley,T.Harnnoi,R.Udomsinprasert,K.Jirajaroenrat, A.J.Ketterman,M.C.Wilce
Key ref:
A.J.Oakley et al. (2001). The crystal structures of glutathione S-transferases isozymes 1-3 and 1-4 from Anopheles dirus species B. Protein Sci, 10, 2176-2185. PubMed id: 11604524 DOI: 10.1110/ps.ps.21201
Date:
16-Jul-01     Release date:   16-Jul-02    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q7KIF1  (Q7KIF1_9DIPT) -  Glutathione transferase
Seq:
Struc:
219 a.a.
217 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.5.1.18  - Glutathione transferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: RX + glutathione = HX + R-S-glutathione
RX
+ glutathione
= HX
+ R-S-glutathione
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   1 term 
  Biochemical function     transferase activity     2 terms  

 

 
    reference    
 
 
DOI no: 10.1110/ps.ps.21201 Protein Sci 10:2176-2185 (2001)
PubMed id: 11604524  
 
 
The crystal structures of glutathione S-transferases isozymes 1-3 and 1-4 from Anopheles dirus species B.
A.J.Oakley, T.Harnnoi, R.Udomsinprasert, K.Jirajaroenrat, A.J.Ketterman, M.C.Wilce.
 
  ABSTRACT  
 
Glutathione S-transferases (GSTs) are dimeric proteins that play an important role in cellular detoxification. Four GSTs from the mosquito Anopheles dirus species B (Ad), an important malaria vector in South East Asia, are produced by alternate splicing of a single transcription product and were previously shown to have detoxifying activity towards pesticides such as DDT. We have determined the crystal structures for two of these alternatively spliced proteins, AdGST1-3 (complexed with glutathione) and AdGST1-4 (apo form), at 1.75 and 2.45 A resolution, respectively. These GST isozymes show differences from the related GST from the Australian sheep blowfly Lucilia cuprina; in particular, the presence of a C-terminal helix forming part of the active site. This helix causes the active site of the Anopheles GSTs to be enclosed. The glutathione-binding helix alpha2 and flanking residues are disordered in the AdGST1-4 (apo) structure, yet ordered in the AdGST1-3 (GSH-bound) structure, suggesting that insect GSTs operate with an induced fit mechanism similar to that found in the plant phi- and human pi-class GSTs. Despite the high overall sequence identities, the active site residues of AdGST1-4 and AdGST1-3 have different conformations.
 
  Selected figure(s)  
 
Figure 2.
Fig. 2. Far UV CD spectra of the wild-type TLL (A) and W89m (B) in 0 (solid square), 25 (open circle) and 50% (x) iPrOH. The concentration of lipases was 0.2 mg/mL, corresponding to 6.7 M, in 20 mM Hepes, 0.1 mM EDTA at pH 7.0. Temperature was 25C.
Figure 3.
Fig. 3. Near UV CD spectra of the wild-type TLL (A) and W89m (B) in 0% (solid square), 25% (open circle) and 50% (x) iPrOH. The concentration of lipases was 1 mg/mL, corresponding to 33.3 M, in 20 mM Hepes, 0.1 mM EDTA at pH 7.0. Temperature was 25C.
 
  The above figures are reprinted by permission from the Protein Society: Protein Sci (2001, 10, 2176-2185) copyright 2001.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20143133 H.Wang (2010).
Characterization of zebrafish Esrom (Myc-binding protein 2) RCC1-like domain splice variants.
  Mol Cell Biochem, 339, 191-199.  
20361049 J.O.Wrabl, and V.J.Hilser (2010).
Investigating homology between proteins using energetic profiles.
  PLoS Comput Biol, 6, e1000722.  
20196771 J.Wongsantichon, R.C.Robinson, and A.J.Ketterman (2010).
Structural contributions of delta class glutathione transferase active-site residues to catalysis.
  Biochem J, 428, 25-32.
PDB codes: 3f63 3f6d 3g7j
19851333 X.X.Ma, Y.L.Jiang, Y.X.He, R.Bao, Y.Chen, and C.Z.Zhou (2009).
Structures of yeast glutathione-S-transferase Gtt2 reveal a new catalytic type of GST family.
  EMBO Rep, 10, 1320-1326.
PDB codes: 3erf 3erg 3ibh
18831774 A.K.Dunker, C.J.Oldfield, J.Meng, P.Romero, J.Y.Yang, J.W.Chen, V.Vacic, Z.Obradovic, and V.N.Uversky (2008).
The unfoldomics decade: an update on intrinsically disordered proteins.
  BMC Genomics, 9, S1.  
18366598 C.J.Oldfield, J.Meng, J.Y.Yang, M.Q.Yang, V.N.Uversky, and A.K.Dunker (2008).
Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners.
  BMC Genomics, 9, S1.  
17331184 B.Ma, and F.N.Chang (2007).
Purification and cloning of a Delta class glutathione S-transferase displaying high peroxidase activity isolated from the German cockroach Blattella germanica.
  FEBS J, 274, 1793-1803.  
17640387 D.Talavera, A.Hospital, M.Orozco, and X.de la Cruz (2007).
A procedure for identifying homologous alternative splicing events.
  BMC Bioinformatics, 8, 260.  
17966126 S.Zheng, H.Deng, T.Ladd, B.L.Tomkins, P.J.Krell, and Q.Feng (2007).
Cloning and characterization of two glutathione S-transferase cDNAs in the spruce budworm, Choristoneura fumiferana.
  Arch Insect Biochem Physiol, 66, 146-157.  
16717195 P.R.Romero, S.Zaidi, Y.Y.Fang, V.N.Uversky, P.Radivojac, C.J.Oldfield, M.S.Cortese, M.Sickmeier, T.LeGall, Z.Obradovic, and A.K.Dunker (2006).
Alternative splicing in concert with protein intrinsic disorder enables increased functional diversity in multicellular organisms.
  Proc Natl Acad Sci U S A, 103, 8390-8395.  
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. Where a reference describes a PDB structure, the PDB codes are shown on the right.