5AN1
Crystallographic structure of the Glutathione S-Transferase from Litopenaeus vannamei complexed with Glutathione
Summary for 5AN1
| Entry DOI | 10.2210/pdb5an1/pdb |
| Descriptor | GLUTATHIONE S-TRANSFERASE, GLUTATHIONE (3 entities in total) |
| Functional Keywords | transferase, glutathione, xenobiotic, disulphide bond gst, mu- class |
| Biological source | LITOPENAEUS VANNAMEI (PACIFIC WHITE SHRIMP) |
| Total number of polymer chains | 8 |
| Total formula weight | 206878.22 |
| Authors | Juarez-Martinez, A.B.,Sotelo-Mundo, R.,Rudino-Pinera, E. (deposition date: 2015-09-02, release date: 2016-10-12, Last modification date: 2024-01-10) |
| Primary citation | Juarez-Martinez, A.B.,Sotelo-Mundo, R.R.,Rudino-Pinera, E. Crystal structure of a class-mu glutathione S-transferase from whiteleg shrimp Litopenaeus vannamei: structural changes in the xenobiotic binding H-site may alter the spectra of molecules bound. J. Biochem. Mol. Toxicol., 31:-, 2017 Cited by PubMed Abstract: Glutathione S-transferases (GSTs) are dimeric proteins that play a key role in phase II cellular detoxification. Here, the first crystal structure of a GST class-mu from marine crustacean shrimp Litopenaeus vannamei is reported at a resolution of 2.0 Å. The coordinates reported here have the lowest sequence identity with previously reported GSTs class-mu deposited at the Protein Data Bank (PDB), although they have subtle conformational differences. One key feature of GST class-mu from L. vannamei is the active site crevice markedly reduced when it is compared with other GSTs class-mu. This finding together with the chemical change of residues into the cavity (F112 and Y210) points to a particular specialization in which smallest xenobiotics with nonstandard chemical characteristics can be bound to the H-site. This suggests that marine organisms have evolved structural strategies to provide efficient selectivity toward xenobiotics to be disposed of by the phase II detoxification process. PubMed: 27717103DOI: 10.1002/jbt.21838 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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