4g10

LigG from Sphingobium sp. SYK-6 is related to the glutathione transferase omega class

spinqualitylabelsall models 4g10, resolution 1.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4g10 is a 1 chain structure with sequence from Sphingomonas paucimobilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.2Å Ligands: ACT, GSH, MSE, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9WXJ9_SPHPI Publication Abstract from PubMed 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 alpha-glutathionyl-beta-hydroxypropiovanillone, argues for broadening the definition of the omega class. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: SpLigG and SpLigGbind by X-ray crystallography (View interaction). Sphingobium sp. SYK-6 LigG involved in lignin degradation is structurally and biochemically related to the glutathione transferase omega class.,Meux E, Prosper P, Masai E, Mulliert G, Dumarcay S, Morel M, Didierjean C, Gelhaye E, Favier F FEBS Lett. 2012 Nov 16;586(22):3944-50. doi: 10.1016/j.febslet.2012.09.036. Epub , 2012 Oct 8. PMID:23058289 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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