3ibh: Difference between revisions

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==Crystal structure of Saccharomyces cerevisiae Gtt2 in complex with glutathione==
==Crystal structure of Saccharomyces cerevisiae Gtt2 in complex with glutathione==
<StructureSection load='3ibh' size='340' side='right' caption='[[3ibh]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='3ibh' size='340' side='right'caption='[[3ibh]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ibh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IBH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3IBH FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ibh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IBH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IBH FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</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]] 2.1&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3erf|3erf]], [[3erg|3erg]]</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></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GTT2, L0560, YLL060C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=3ibh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ibh OCA], [https://pdbe.org/3ibh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ibh RCSB], [https://www.ebi.ac.uk/pdbsum/3ibh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ibh ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ibh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ibh OCA], [http://pdbe.org/3ibh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ibh RCSB], [http://www.ebi.ac.uk/pdbsum/3ibh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ibh ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GST2_YEAST GST2_YEAST]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ib/3ibh_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ib/3ibh_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
Line 31: Line 31:


==See Also==
==See Also==
*[[Glutathione S-transferase|Glutathione S-transferase]]
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Glutathione transferase]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Bao, R]]
[[Category: Bao R]]
[[Category: Chen, Y X]]
[[Category: Chen YX]]
[[Category: He, Y X]]
[[Category: He YX]]
[[Category: Jiang, Y L]]
[[Category: Jiang YL]]
[[Category: Ma, X X]]
[[Category: Ma XX]]
[[Category: Zhou, C Z]]
[[Category: Zhou CZ]]
[[Category: Glutathione s-transferase]]
[[Category: Transferase]]

Latest revision as of 18:57, 1 November 2023

Crystal structure of Saccharomyces cerevisiae Gtt2 in complex with glutathioneCrystal structure of Saccharomyces cerevisiae Gtt2 in complex with glutathione

Structural highlights

3ibh is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GST2_YEAST

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

Glutathione-S-transferases (GSTs) are ubiquitous detoxification enzymes that catalyse the conjugation of electrophilic substrates to glutathione. Here, we present the crystal structures of Gtt2, a GST of Saccharomyces cerevisiae, in apo and two ligand-bound forms, at 2.23 A, 2.20 A and 2.10 A, respectively. Although Gtt2 has the overall structure of a GST, the absence of the classic catalytic essential residues--tyrosine, serine and cysteine--distinguishes it from all other cytosolic GSTs of known structure. Site-directed mutagenesis in combination with activity assays showed that instead of the classic catalytic residues, a water molecule stabilized by Ser129 and His123 acts as the deprotonator of the glutathione sulphur atom. Furthermore, only glycine and alanine are allowed at the amino-terminus of helix-alpha1 because of stereo-hindrance. Taken together, these results show that yeast Gtt2 is a novel atypical type of cytosolic GST.

Structures of yeast glutathione-S-transferase Gtt2 reveal a new catalytic type of GST family.,Ma XX, Jiang YL, He YX, Bao R, Chen Y, Zhou CZ EMBO Rep. 2009 Dec;10(12):1320-6. Epub 2009 Oct 23. PMID:19851333[1]

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

See Also

References

  1. Ma XX, Jiang YL, He YX, Bao R, Chen Y, Zhou CZ. Structures of yeast glutathione-S-transferase Gtt2 reveal a new catalytic type of GST family. EMBO Rep. 2009 Dec;10(12):1320-6. Epub 2009 Oct 23. PMID:19851333 doi:10.1038/embor.2009.216

3ibh, resolution 2.10Å

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OCA