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16gs
From Proteopedia
| 16gs, resolution 1.90Å () | |||||||||
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| Ligands: | , | ||||||||
| Gene: | GSTP1 (Homo sapiens) | ||||||||
| Activity: | Glutathione transferase, with EC number 2.5.1.18 | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 3
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.
Evidence for an induced-fit mechanism operating in pi class glutathione transferases., Oakley AJ, Lo Bello M, Ricci G, Federici G, Parker MW, Biochemistry. 1998 Jul 14;37(28):9912-7. PMID:9665696
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
16gs is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Oakley AJ, Lo Bello M, Ricci G, Federici G, Parker MW. Evidence for an induced-fit mechanism operating in pi class glutathione transferases. Biochemistry. 1998 Jul 14;37(28):9912-7. PMID:9665696 doi:10.1021/bi980323w
