4G10
LigG from Sphingobium sp. SYK-6 is related to the glutathione transferase omega class
Summary for 4G10
| Entry DOI | 10.2210/pdb4g10/pdb |
| Descriptor | Glutathione S-transferase homolog, GLUTATHIONE, ACETATE ION, ... (5 entities in total) |
| Functional Keywords | thioredoxin fold, transferase |
| Biological source | Sphingomonas paucimobilis |
| Total number of polymer chains | 1 |
| Total formula weight | 31202.97 |
| Authors | Meux, E.,Prosper, P.,Masai, E.,Mulliert Carlin, G.,Dumarcay, S.,Morel, M.,Didierjean, C.,Gelhaye, E.,Favier, F. (deposition date: 2012-07-10, release date: 2012-10-03, Last modification date: 2017-11-15) |
| Primary citation | Meux, E.,Prosper, P.,Masai, E.,Mulliert, G.,Dumarcay, S.,Morel, M.,Didierjean, C.,Gelhaye, E.,Favier, F. Sphingobium sp. SYK-6 LigG involved in lignin degradation is structurally and biochemically related to the glutathione transferase omega class. Febs Lett., 586:3944-3950, 2012 Cited by PubMed Abstract: SpLigG is one of the three glutathione transferases (GSTs) involved in the process of lignin breakdown in the soil bacterium Sphingobium sp. SYK-6. Sequence comparisons showed that SpLigG and several proteobacteria homologues form an independent cluster within cysteine-containing GSTs. The relationship between SpLigG and other GSTs was investigated. The X-ray structure and biochemical properties of SpLigG indicate that this enzyme belongs to the omega class of glutathione transferases. However, the hydrophilic substrate binding site of SpLigG, together with its known ability to stereoselectively deglutathionylate the physiological substrate α-glutathionyl-β-hydroxypropiovanillone, argues for broadening the definition of the omega class. PubMed: 23058289DOI: 10.1016/j.febslet.2012.09.036 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.2 Å) |
Structure validation
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