5LKD: Crystal structure of the Xi glutathione transferase ECM4 from Saccharomyces cerevisiae in complex with glutathione

Citation:
Abstract
Glutathionyl-hydroquinone reductases (GHRs) belong to the recently characterized Xi-class of glutathione transferases (GSTXs) according to unique structural properties and are present in all but animal kingdoms. The GHR ScECM4 from the yeast Saccharomyces cerevisiae has been studied since 1997 when it was found to be potentially involved in cell-wall biosynthesis. Up to now and in spite of biological studies made on this enzyme, its physiological role remains challenging. The work here reports its crystallographic study. In addition to exhibiting the general GSTX structural features, ScECM4 shows extensions including a huge loop which contributes to the quaternary assembly. These structural extensions are probably specific to Saccharomycetaceae. Soaking of ScECM4 crystals with GS-menadione results in a structure where glutathione forms a mixed disulfide bond with the cysteine 46. Solution studies confirm that ScECM4 has reductase activity for GS-menadione in presence of glutathione. Moreover, the high resolution structures allowed us to propose new roles of conserved residues of the active site to assist the cysteine 46 during the catalytic act.
PDB ID: 5LKDDownload
MMDB ID: 144415
PDB Deposition Date: 2016/7/22
Updated in MMDB: 2016/10
Experimental Method:
x-ray diffraction
Resolution: 1.68  Å
Source Organism:
Similar Structures:
Biological Unit for 5LKD: dimeric; determined by software (PISA)
Molecular Components in 5LKD
Label Count Molecule
Proteins (2 molecules)
2
Glutathione S-transferase Omega-like 2(Gene symbol: ECM4)
Molecule annotation
Chemicals (2 molecules)
1
2
* Click molecule labels to explore molecular sequence information.

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