| General information | | DisProt: | DP00731 | | Name: | Glutathione S-transferase alpha-1 | | Synonym(s): | GSTA1_RAT
GST 1-1
GST 1a-1a
GST A1-1
GST B
Glutathione S-transferase Ya-1
Ligandin
GST Ya1
| | First appeared in release: | Release 6.01 (10/15/2012) | | UniProt: | P00502 | | UniGene: | | | SwissProt: | GSTA1_RAT | | TrEMBL: | | | NCBI (GI): | | | Source organism: | Rattus norvegicus (Rat) | | Sequence length: | 222 | | Percent disordered: | 6% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
| | | | | |
MSGKPVLHYF NARGRMECIR WLLAAAGVEF DEKFIQSPED LEKLKKDGNL MFDQVPMVEI - 60
DGMKLAQTRA ILNYIATKYD LYGKDMKERA LIDMYTEGIL DLTEMIMQLV ICPPDQKEAK - 120
TALAKDRTKN RYLPAFEKVL KSHGQDYLVG NRLTRVDIHL LELLLYVEEF DASLLTSFPL - 180
LKAFKSRISS LPNVKKFLQP GSQRKLPVDA KQIEEARKIF KF
|
| Functional narrative |
Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
SUBUNIT: Homodimer.
Subcellular Location: Cytoplasm.
MISCELLANEOUS: In addition to its enzymatic activity, the homodimer of Ya chains, called ligandin, binds various organic anions, xenobiotics, and azocarcinogen dyes.
SIMILARITY: Belongs to the GST superfamily. Alpha family.
SIMILARITY: Contains 1 GST C-terminal domain.
SIMILARITY: Contains 1 GST N-terminal domain.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
|
| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
|
| Region 1 | | Type: | Disordered | | Name: | C-terminal region | | Location: | 210 - 222 | | Length: | 13 | | Region sequence: |
AKQIEEARKIFKF | | Modification type: | Mutant
| | PDB: | 1EV4:A, 1EV9:A | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Intraprotein interaction
Substrate/ligand binding
| Detection methods:
- X-ray crystallography (298 K; pH: 10.5; 3-cyclohexylamino-1-propane sulfonic acid (CAPS) 0.1 M; GSTA1-1 protein (W21F mutant (PDB 1EV9)) 10 mg/mL; lithium sulfate 0.2 M; saturated ammonium sulfate 50 %)
- X-ray crystallography (298 K; pH: 6.5; GSTA1-1 protein (W21F, F220Y mutant (PDB 1EV4)) 10 mg/mL; HEPES 0.1 M; saturated ammonium sulfate 60 %; S-hexyl glutathione 1 mM)
- Fluorescence polarization/anisotropy (298 K; pH: 6.5; GSH, GS-EA, GSO3-, S-hexyl GSH or EA (0.2 to 200uM); GST protein (F222W mutant) 2 uM; MES (buffer) 100 mM)
| References:
- Adman ET, Le Trong I, Stenkamp RE, Nieslanik BS, Dietze EC, Tai G, Ibarra C, Atkins WM. "Localization of the C-terminus of rat glutathione S-transferase A1-1: crystal structure of mutants W21F and W21F/F220Y." Proteins. 2001; 42(2): 192-200. PubMed: 11119643
| Comments:
|
| Comments |
AV sent 10/1/2012 (PMID:11119643)
|
| If you have any comments or wish to provide additional references to this protein or its disordered region(s), please click here to e-mail us. |
Disprot-footer
|
