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PDBsum entry 1mtc

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protein ligands Protein-protein interface(s) links
Transferase PDB id
1mtc
Jmol
Contents
Protein chains
217 a.a. *
Ligands
GPR ×2
Waters ×185
* Residue conservation analysis
PDB id:
1mtc
Name: Transferase
Title: Glutathione transferase mutant y115f
Structure: Glutathione s-transferase yb1. Chain: a, b. Synonym: chain 3. Gst m1-1. Gst class-mu 1. Glutathione s- transferase yb-1 subunit. Engineered: yes. Mutation: yes. Other_details: complex with (9r,10r)-9-(s-glutathionyl)-10- hydroxy-9,10-dihrophenanthrene
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Organ: liver. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PQS)
Resolution:
2.20Å     R-factor:   0.203    
Authors: J.E.Ladner,G.Xiao,R.N.Armstrong,G.L.Gilliland
Key ref:
S.G.Codreanu et al. (2002). Local protein dynamics and catalysis: detection of segmental motion associated with rate-limiting product release by a glutathione transferase. Biochemistry, 41, 15161-15172. PubMed id: 12484753 DOI: 10.1021/bi026776p
Date:
20-Sep-02     Release date:   25-Mar-03    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P04905  (GSTM1_RAT) -  Glutathione S-transferase Mu 1
Seq:
Struc:
218 a.a.
217 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 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
Bound ligand (Het Group name = GPR)
matches with 57.00% similarity
= 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     extracellular region   3 terms 
  Biological process     metabolic process   12 terms 
  Biochemical function     transferase activity     5 terms  

 

 
    reference    
 
 
DOI no: 10.1021/bi026776p Biochemistry 41:15161-15172 (2002)
PubMed id: 12484753  
 
 
Local protein dynamics and catalysis: detection of segmental motion associated with rate-limiting product release by a glutathione transferase.
S.G.Codreanu, J.E.Ladner, G.Xiao, N.V.Stourman, D.L.Hachey, G.L.Gilliland, R.N.Armstrong.
 
  ABSTRACT  
 
Glutathione transferase rGSTM1-1 catalyzes the addition of glutathione (GSH) to 1-chloro-2,4-dinitrobenzene, a reaction in which the chemical step is 60-fold faster than the physical step of product release. The hydroxyl group of Y115, located in the active site access channel, controls the egress of product from the active site. The Y115F mutant enzyme has a k(cat) (72 s(-)(1)) that is 3.6-fold larger than that of the native enzyme (20 s(-)(1)). Crystallographic observations and evidence from amide proton exchange kinetics are consistent with localized increases in the degree of segmental motion of the Y115F mutant that are coupled to the enhanced rate of product release. The loss of hydrogen bonding interactions involving the hydroxyl group of Y115 is reflected in subtle alterations in the backbone position, an increase in B-factors for structural elements that comprise the channel to the active site, and, most dramatically, a loss of well-defined electron density near the site of mutation. The kinetics of amide proton exchange are also enhanced by a factor between 3 and 12 in these regions, providing direct, quantitative evidence for changes in local protein dynamics affecting product release. The enhanced product release rate is proposed to derive from a small shift in the equilibrium population of protein conformers that permit egress of the product from the active site.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19170039 S.J.Coales, S.J.Tuske, J.C.Tomasso, and Y.Hamuro (2009).
Epitope mapping by amide hydrogen/deuterium exchange coupled with immobilization of antibody, on-line proteolysis, liquid chromatography and mass spectrometry.
  Rapid Commun Mass Spectrom, 23, 639-647.  
18939839 A.J.Smith, R.Müller, M.D.Toscano, P.Kast, H.W.Hellinga, D.Hilvert, and K.N.Houk (2008).
Structural reorganization and preorganization in enzyme active sites: comparisons of experimental and theoretically ideal active site geometries in the multistep serine esterase reaction cycle.
  J Am Chem Soc, 130, 15361-15373.  
18703268 N.Kinsley, Y.Sayed, S.Mosebi, R.N.Armstrong, and H.W.Dirr (2008).
Characterization of the binding of 8-anilinonaphthalene sulfonate to rat class Mu GST M1-1.
  Biophys Chem, 137, 100-104.  
18381619 S.J.Coales, J.C.Tomasso, and Y.Hamuro (2008).
Effects of electrospray capillary temperature on amide hydrogen exchange.
  Rapid Commun Mass Spectrom, 22, 1367-1371.  
17561509 L.Hou, M.T.Honaker, L.M.Shireman, L.M.Balogh, A.G.Roberts, K.C.Ng, A.Nath, and W.M.Atkins (2007).
Functional promiscuity correlates with conformational heterogeneity in A-class glutathione S-transferases.
  J Biol Chem, 282, 23264-23274.  
17088323 J.A.Butterwick, and A.G.Palmer (2006).
An inserted Gly residue fine tunes dynamics between mesophilic and thermophilic ribonucleases H.
  Protein Sci, 15, 2697-2707.  
16672236 J.L.Hearne, and R.F.Colman (2006).
Contribution of the mu loop to the structure and function of rat glutathione transferase M1-1.
  Protein Sci, 15, 1277-1289.  
14726533 J.Lengqvist, R.Svensson, E.Evergren, R.Morgenstern, and W.J.Griffiths (2004).
Observation of an intact noncovalent homotrimer of detergent-solubilized rat microsomal glutathione transferase-1 by electrospray mass spectrometry.
  J Biol Chem, 279, 13311-13316.  
12637518 C.A.Ibarra, P.Chowdhury, J.W.Petrich, and W.M.Atkins (2003).
The anomalous pKa of Tyr-9 in glutathione S-transferase A1-1 catalyzes product release.
  J Biol Chem, 278, 19257-19265.  
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.