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1yzx
From Proteopedia
| Line 5: | Line 5: | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=GSF:L-GAMMA-GLUTAMYL-3-SULFINO-L-ALANYLGLYCINE'>GSF</scene> | |LIGAND= <scene name='pdbligand=GSF:L-GAMMA-GLUTAMYL-3-SULFINO-L-ALANYLGLYCINE'>GSF</scene> | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yzx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yzx OCA], [http://www.ebi.ac.uk/pdbsum/1yzx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yzx RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Li, J.]] | [[Category: Li, J.]] | ||
[[Category: Xia, Z.]] | [[Category: Xia, Z.]] | ||
| - | [[Category: GSF]] | ||
[[Category: glutathione sulfinate]] | [[Category: glutathione sulfinate]] | ||
[[Category: peroxidase]] | [[Category: peroxidase]] | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:27:10 2008'' |
Revision as of 22:27, 30 March 2008
| |||||||
| , resolution 1.93Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Glutathione transferase, with EC number 2.5.1.18 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of human kappa class glutathione transferase
Overview
Glutathione transferases (GSTs) are a superfamily of enzymes that play a vital functional role in the cellular detoxification process. They catalyze the conjugation of the thiol group of glutathione (GSH) to the electrophilic groups of a wide range of hydrophobic substrates, leading to an easier removal of the latter from the cells. The kappa class is the least studied one among various classes within the superfamily. We report here the expression, purification, and crystal structure of human kappa class GST (hGSTK), which has been determined by the multiple-isomorphous replacement method and refined to 1.93 A resolution. The overall structure of hGSTK is similar to the recently reported structure of kappa class GST from rat mitochondrion. Each subunit of the dimeric hGSTK contains a thioredoxin (TRX)-like domain and a helical domain. A molecule of glutathione sulfinate, an oxidized product of GSH, is found to bind at the G site of each monomer. One oxygen atom of the sulfino group of GSF forms a hydrogen bond with the hydroxyl group of the catalytic residue Ser16. The TRX-like domain of hGSTK shares 19% sequence identity and structure similarity with human theta class GST, suggesting that the kappa class of GST is more closely related to the theta class enzyme within the GST superfamily. The structure of the TRX-like domain of hGSTK is also similar to that of glutathione peroxidase (GPx), implying an evolutionary relationship between GST and GPx.
About this Structure
1YZX is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Thioredoxin-like domain of human kappa class glutathione transferase reveals sequence homology and structure similarity to the theta class enzyme., Li J, Xia Z, Ding J, Protein Sci. 2005 Sep;14(9):2361-9. Epub 2005 Aug 4. PMID:16081649
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