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2ca8

From Proteopedia

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Current revision

Structure of Sh28GST in complex with GSH at pH 6.0

Structural highlights

2ca8 is a 1 chain structure with sequence from Schistosoma haematobium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.49Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GST28_SCHBO Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

During turnover, the catalytic tyrosine residue (Tyr10) of the sigma class Schistosoma haematobium wild-type glutathione-S-transferase is expected to switch alternately in and out of the reduced glutathione-binding site (G-site). The Tyrout10 conformer forms a pi-cation interaction with the guanidinium group of Arg21. As in other similar glutathione-S-transferases, the catalytic Tyr has a low pKa of 7.2. In order to investigate the catalytic role of Tyr10, and the structural and functional roles of Arg21, we carried out structural studies on two Arg21 mutants (R21L and R21Q) and a Tyr10 mutant, Y10F. Our crystallographic data for the two Arg21 mutants indicate that only the Tyrout10 conformation is populated, thereby excluding a role of Arg21 in the stabilisation of the out conformation. However, Arg21 was confirmed to be catalytically important and essential for the low pKa of Tyr10. Upon comparison with structural data generated for reduced glutathione-bound and inhibitor-bound wild-type enzymes, it was observed that the orientations of Tyr10 and Arg35 are concerted and that, upon ligand binding, minor rearrangements occur within conserved residues in the active site loop. These rearrangements are coupled to quaternary rigid-body movements at the dimer interface and alterations in the localisation and structural order of the C-terminal domain.

Probing the mechanism of GSH activation in Schistosoma haematobium glutathione-S-transferase by site-directed mutagenesis and X-ray crystallography.,Baiocco P, Gourlay LJ, Angelucci F, Fontaine J, Herve M, Miele AE, Trottein F, Brunori M, Bellelli A J Mol Biol. 2006 Jul 14;360(3):678-89. Epub 2006 Jun 2. PMID:16777141^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Baiocco P, Gourlay LJ, Angelucci F, Fontaine J, Herve M, Miele AE, Trottein F, Brunori M, Bellelli A. Probing the mechanism of GSH activation in Schistosoma haematobium glutathione-S-transferase by site-directed mutagenesis and X-ray crystallography. J Mol Biol. 2006 Jul 14;360(3):678-89. Epub 2006 Jun 2. PMID:16777141 doi:10.1016/j.jmb.2006.05.040

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ca8"

@@ Line 3: / Line 3: @@
 <StructureSection load='2ca8' size='340' side='right'caption='[[2ca8]], [[Resolution|resolution]] 2.49&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ca8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Blood_fluke Blood fluke]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CA8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CA8 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ca8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Schistosoma_haematobium Schistosoma haematobium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CA8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CA8 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.49&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2c80|2c80]], [[2c8u|2c8u]], [[2cai|2cai]], [[2caq|2caq]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </span></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ca8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ca8 OCA], [https://pdbe.org/2ca8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ca8 RCSB], [https://www.ebi.ac.uk/pdbsum/2ca8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ca8 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/GST28_SCHBO GST28_SCHBO]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.  GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.
+[https://www.uniprot.org/uniprot/GST28_SCHBO GST28_SCHBO] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.  GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 37: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Blood fluke]]
-[[Category: Glutathione transferase]]
 [[Category: Large Structures]]
-[[Category: Angelucci, F]]
+[[Category: Schistosoma haematobium]]
-[[Category: Baiocco, P]]
+[[Category: Angelucci F]]
-[[Category: Bellelli, A]]
+[[Category: Baiocco P]]
-[[Category: Brunori, M]]
+[[Category: Bellelli A]]
-[[Category: Gourlay, L J]]
+[[Category: Brunori M]]
-[[Category: Miele, A E]]
+[[Category: Gourlay LJ]]
-[[Category: Detoxification]]
+[[Category: Miele AE]]
-[[Category: Glutathione]]
-[[Category: Prostaglandin d2 synthase]]
-[[Category: Sigma class gst]]
-[[Category: Transferase]]

2ca8

From Proteopedia

Current revision

Structure of Sh28GST in complex with GSH at pH 6.0

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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