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PDBsum entry 16gs

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protein ligands Protein-protein interface(s) links
Transferase PDB id
16gs
Jmol
Contents
Protein chain
208 a.a. *
Ligands
SO4
MES ×2
Waters ×298
* Residue conservation analysis
PDB id:
16gs
Name: Transferase
Title: Glutathione s-transferase p1-1 apo form 3
Structure: Glutathione s-transferase. Chain: a, b. Synonym: gstp1-1. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Cellular_location: cytosol. Gene: gstp1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PDB file)
Resolution:
1.90Å     R-factor:   0.227     R-free:   0.263
Authors: A.J.Oakley,M.Lo Bello,G.Ricci,G.Federici,M.W.Parker
Key ref:
A.J.Oakley et al. (1998). Evidence for an induced-fit mechanism operating in pi class glutathione transferases. Biochemistry, 37, 9912-9917. PubMed id: 9665696 DOI: 10.1021/bi980323w
Date:
30-Nov-97     Release date:   13-Jan-99    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P09211  (GSTP1_HUMAN) -  Glutathione S-transferase P
Seq:
Struc:
210 a.a.
208 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!
  Cellular component     TRAF2-GSTP1 complex   9 terms 
  Biological process     metabolic process   31 terms 
  Biochemical function     S-nitrosoglutathione binding     8 terms  

 

 
    reference    
 
 
DOI no: 10.1021/bi980323w Biochemistry 37:9912-9917 (1998)
PubMed id: 9665696  
 
 
Evidence for an induced-fit mechanism operating in pi class glutathione transferases.
A.J.Oakley, M.Lo Bello, G.Ricci, G.Federici, M.W.Parker.
 
  ABSTRACT  
 
Three-dimensional structures of the apo form of human pi class glutathione transferase have been determined by X-ray crystallography. The structures suggest the enzyme recognizes its substrate, glutathione, by an induced-fit mechanism. Compared to complexed forms of the enzyme, the environment around the catalytic residue, Tyr 7, remains unchanged in the apoenzyme. This observation supports the view that Tyr 7 does not act as a general base in the reaction mechanism. The observed cooperativity of the dimeric enzyme may be due to the movements of a helix that forms one wall of the active site and, in particular, to movements of a tyrosine residue that is located in the subunit interface.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20540076 I.Quesada-Soriano, L.J.Parker, A.Primavera, J.Wielens, J.K.Holien, J.M.Casas-Solvas, A.Vargas-Berenguel, A.M.Aguilera, M.Nuccetelli, A.P.Mazzetti, M.L.Bello, M.W.Parker, and L.García-Fuentes (2011).
Diuretic drug binding to human glutathione transferase P1-1: potential role of Cys-101 revealed in the double mutant C47S/Y108V.
  J Mol Recognit, 24, 220-234.
PDB codes: 3km6 3kmo
19217864 D.Long, and D.Yang (2009).
Buffer interference with protein dynamics: a case study on human liver fatty acid binding protein.
  Biophys J, 96, 1482-1488.  
18790135 Q.Zhang, E.Crosland, and D.Fabris (2008).
Nested Arg-specific bifunctional crosslinkers for MS-based structural analysis of proteins and protein assemblies.
  Anal Chim Acta, 627, 117-128.  
16597834 R.Téllez-Sanz, E.Cesareo, M.Nuccetelli, A.M.Aguilera, C.Barón, L.J.Parker, J.J.Adams, C.J.Morton, M.Lo Bello, M.W.Parker, and L.García-Fuentes (2006).
Calorimetric and structural studies of the nitric oxide carrier S-nitrosoglutathione bound to human glutathione transferase P1-1.
  Protein Sci, 15, 1093-1105.
PDB codes: 2a2r 2a2s
16154081 F.Angelucci, P.Baiocco, M.Brunori, L.Gourlay, V.Morea, and A.Bellelli (2005).
Insights into the catalytic mechanism of glutathione S-transferase: the lesson from Schistosoma haematobium.
  Structure, 13, 1241-1246.  
15772311 M.I.Zavodszky, and L.A.Kuhn (2005).
Side-chain flexibility in protein-ligand binding: the minimal rotation hypothesis.
  Protein Sci, 14, 1104-1114.  
15640152 M.Perbandt, J.Höppner, C.Betzel, R.D.Walter, and E.Liebau (2005).
Structure of the major cytosolic glutathione S-transferase from the parasitic nematode Onchocerca volvulus.
  J Biol Chem, 280, 12630-12636.
PDB codes: 1tu7 1tu8
  17597848 R.Bhargavi, S.Vishwakarma, and U.S.Murty (2005).
Modeling analysis of GST (glutathione-S-transferases) from Wuchereria bancrofti and Brugia malayi.
  Bioinformation, 1, 25-27.  
15347687 L.A.Ralat, and R.F.Colman (2004).
Glutathione S-transferase Pi has at least three distinguishable xenobiotic substrate sites close to its glutathione-binding site.
  J Biol Chem, 279, 50204-50213.  
14676193 U.M.Hegazy, B.Mannervik, and G.Stenberg (2004).
Functional role of the lock and key motif at the subunit interface of glutathione transferase p1-1.
  J Biol Chem, 279, 9586-9596.  
12937169 E.Ortiz-Salmerón, M.Nuccetelli, A.J.Oakley, M.W.Parker, M.Lo Bello, and L.García-Fuentes (2003).
Thermodynamic description of the effect of the mutation Y49F on human glutathione transferase P1-1 in binding with glutathione and the inhibitor S-hexylglutathione.
  J Biol Chem, 278, 46938-46948.
PDB code: 22gs
14573868 L.A.Ralat, and R.F.Colman (2003).
Monobromobimane occupies a distinct xenobiotic substrate site in glutathione S-transferase pi.
  Protein Sci, 12, 2575-2587.  
11604524 A.J.Oakley, T.Harnnoi, R.Udomsinprasert, K.Jirajaroenrat, A.J.Ketterman, and M.C.Wilce (2001).
The crystal structures of glutathione S-transferases isozymes 1-3 and 1-4 from Anopheles dirus species B.
  Protein Sci, 10, 2176-2185.
PDB codes: 1jlv 1jlw
11123923 C.Micaloni, A.P.Mazzetti, M.Nuccetelli, J.Rossjohn, W.J.McKinstry, G.Antonini, A.M.Caccuri, A.J.Oakley, G.Federici, G.Ricci, M.W.Parker, and M.Lo Bello (2000).
Valine 10 may act as a driver for product release from the active site of human glutathione transferase P1-1.
  Biochemistry, 39, 15961-15970.  
10858281 S.A.McCallum, T.K.Hitchens, C.Torborg, and G.S.Rule (2000).
Ligand-induced changes in the structure and dynamics of a human class Mu glutathione S-transferase.
  Biochemistry, 39, 7343-7356.  
10383436 A.M.Caccuri, G.Antonini, P.Ascenzi, M.Nicotra, M.Nuccetelli, A.P.Mazzetti, G.Federici, M.Lo Bello, and G.Ricci (1999).
Temperature adaptation of glutathione S-transferase P1-1. A case for homotropic regulation of substrate binding.
  J Biol Chem, 274, 19276-19280.  
10451546 L.Stella, E.E.Di Iorio, M.Nicotra, and G.Ricci (1999).
Molecular dynamics simulations of human glutathione transferase P1-1: conformational fluctuations of the apo-structure.
  Proteins, 37, 10-19.  
10451545 L.Stella, M.Nicotra, G.Ricci, N.Rosato, and E.E.Di Iorio (1999).
Molecular dynamics simulations of human glutathione transferase P1-1: analysis of the induced-fit mechanism by GSH binding.
  Proteins, 37, 1-9.  
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.