3f6d: Difference between revisions

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-{{Seed}}
-[[Image:3f6d.png|left|200px]]
-<!--
+==Crystal Structure of a Genetically Modified Delta Class GST (adGSTD4-4) from Anopheles dirus, F123A, in Complex with S-Hexyl Glutathione==
-The line below this paragraph, containing "STRUCTURE_3f6d", creates the "Structure Box" on the page.
+<StructureSection load='3f6d' size='340' side='right'caption='[[3f6d]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3f6d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Anopheles_dirus Anopheles dirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F6D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3F6D FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTX:S-HEXYLGLUTATHIONE'>GTX</scene></td></tr>
-{{STRUCTURE_3f6d|  PDB=3f6d  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3f6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f6d OCA], [https://pdbe.org/3f6d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3f6d RCSB], [https://www.ebi.ac.uk/pdbsum/3f6d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3f6d ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q9GN60_9DIPT Q9GN60_9DIPT]
+== 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/f6/3f6d_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=3f6d ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+GST (glutathione transferase) is a dimeric enzyme recognized for biotransformation of xenobiotics and endogenous toxic compounds. In the present study, residues forming the hydrophobic substrate-binding site (H-site) of a Delta class enzyme were investigated in detail for the first time by site-directed mutagenesis and crystallographic studies. Enzyme kinetics reveal that Tyr111 indirectly stabilizes GSH binding, Tyr119 modulates hydrophobic substrate binding and Phe123 indirectly modulates catalysis. Mutations at Tyr111 and Phe123 also showed evidence for positive co-operativity for GSH and 1-chloro-2,4-dinitrobenzene respectively, strongly suggesting a role for these residues in manipulating subunit-subunit communication. In the present paper we report crystal structures of the wild-type enzyme, and two mutants, in complex with S-hexylglutathione. This study has identified an aromatic 'zipper' in the H-site contributing a network of aromatic pi-pi interactions. Several residues of the cluster directly interact with the hydrophobic substrate, whereas others indirectly maintain conformational stability of the dimeric structure through the C-terminal domain (domain II). The Y119E mutant structure shows major main-chain rearrangement of domain II. This reorganization is moderated through the 'zipper' that contributes to the H-site remodelling, thus illustrating a role in co-substrate binding modulation. The F123A structure shows molecular rearrangement of the H-site in one subunit, but not the other, explaining weakened hydrophobic substrate binding and kinetic co-operativity effects of Phe123 mutations. The three crystal structures provide comprehensive evidence of the aromatic 'zipper' residues having an impact upon protein stability, catalysis and specificity. Consequently, 'zipper' residues appear to modulate and co-ordinate substrate processing through permissive flexing.
-===Crystal Structure of a Genetically Modified Delta Class GST (adGSTD4-4) from Anopheles dirus, F123A, in Complex with S-Hexyl Glutathione===
+Structural contributions of delta class glutathione transferase active-site residues to catalysis.,Wongsantichon J, Robinson RC, Ketterman AJ Biochem J. 2010 Apr 28;428(1):25-32. PMID:20196771<ref>PMID:20196771</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3f6d" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_20196771}}, adds the Publication Abstract to the page
+*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 20196771 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_20196771}}
+__TOC__
+</StructureSection>
-==About this Structure==
-F6D is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Anopheles_dirus Anopheles dirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F6D OCA].
-==Reference==
-<ref group="xtra">PMID:20196771</ref><references group="xtra"/>
 [[Category: Anopheles dirus]]
-[[Category: Glutathione transferase]]
+[[Category: Large Structures]]
-[[Category: Ketterman, A J.]]
+[[Category: Ketterman AJ]]
-[[Category: Robinson, R C.]]
+[[Category: Robinson RC]]
-[[Category: Wongsantichon, J.]]
+[[Category: Wongsantichon J]]
-[[Category: Glutathione transferase]]
-[[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 12 10:27:18 2010''