2pvq
From Proteopedia
(Difference between revisions)
| (14 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:2pvq.jpg|left|200px]]<br /><applet load="2pvq" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2pvq, resolution 1.803Å" /> | ||
| - | '''Crystal structure of Ochrobactrum anthropi glutathione transferase Cys10Ala mutant with glutathione bound at the H-site'''<br /> | ||
| - | == | + | ==Crystal structure of Ochrobactrum anthropi glutathione transferase Cys10Ala mutant with glutathione bound at the H-site== |
| + | <StructureSection load='2pvq' size='340' side='right'caption='[[2pvq]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2pvq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Brucella_anthropi Brucella anthropi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PVQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PVQ FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.803Å</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=SO4:SULFATE+ION'>SO4</scene></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=2pvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pvq OCA], [https://pdbe.org/2pvq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pvq RCSB], [https://www.ebi.ac.uk/pdbsum/2pvq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pvq ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/GST_BRUAN GST_BRUAN] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pv/2pvq_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2pvq ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The role of the evolutionarily conserved residue Cys10 in Ochrobactrum anthropi glutathione transferase (OaGST) has been examined by replacing it with an alanine. A double mutant C10A/S11A was also prepared. The effect of the replacements on the coniugating and thiotransferase activities, and on the thermal and chemical stability of the enzyme was analyzed. Our data support the view that in OaGST, in contrast with other beta class GSTs that display significant differences in the glutathione-binding site, Cys10 is a key residue for glutathione coniugating activity. Furthermore, analysis of the OaGST-Cys10Ala structure, crystallized in the presence of glutathione, reveals that this mutation causes a switch between the high-affinity G-site and a low-affinity H-site where hydrophobic cosubstrates bind and where we observe the presence of an unexpected glutathione. Proteins 2008. (c) 2007 Wiley-Liss, Inc. | The role of the evolutionarily conserved residue Cys10 in Ochrobactrum anthropi glutathione transferase (OaGST) has been examined by replacing it with an alanine. A double mutant C10A/S11A was also prepared. The effect of the replacements on the coniugating and thiotransferase activities, and on the thermal and chemical stability of the enzyme was analyzed. Our data support the view that in OaGST, in contrast with other beta class GSTs that display significant differences in the glutathione-binding site, Cys10 is a key residue for glutathione coniugating activity. Furthermore, analysis of the OaGST-Cys10Ala structure, crystallized in the presence of glutathione, reveals that this mutation causes a switch between the high-affinity G-site and a low-affinity H-site where hydrophobic cosubstrates bind and where we observe the presence of an unexpected glutathione. Proteins 2008. (c) 2007 Wiley-Liss, Inc. | ||
| - | + | Cysteine 10 is critical for the activity of Ochrobactrum anthropi glutathione transferase and its mutation to alanine causes the preferential binding of glutathione to the H-site.,Allocati N, Federici L, Masulli M, Favaloro B, Di Ilio C Proteins. 2007 Dec 12;71(1):16-23. PMID:18076047<ref>PMID:18076047</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2pvq" style="background-color:#fffaf0;"></div> | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ==See Also== | |
| + | *[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Brucella anthropi]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Allocati N]] | ||
| + | [[Category: Di Ilio C]] | ||
| + | [[Category: Favaloro B]] | ||
| + | [[Category: Federici L]] | ||
| + | [[Category: Masulli M]] | ||
Current revision
Crystal structure of Ochrobactrum anthropi glutathione transferase Cys10Ala mutant with glutathione bound at the H-site
| |||||||||||
