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3vk9

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==Crystal structure of delta-class glutathione transferase from silkmoth==
==Crystal structure of delta-class glutathione transferase from silkmoth==
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<StructureSection load='3vk9' size='340' side='right' caption='[[3vk9]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='3vk9' size='340' side='right'caption='[[3vk9]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3vk9]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bommo Bommo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VK9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VK9 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3vk9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VK9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VK9 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.001&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GST delta ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7091 BOMMO])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vk9 OCA], [https://pdbe.org/3vk9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vk9 RCSB], [https://www.ebi.ac.uk/pdbsum/3vk9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vk9 ProSAT]</span></td></tr>
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<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=3vk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vk9 OCA], [http://pdbe.org/3vk9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vk9 RCSB], [http://www.ebi.ac.uk/pdbsum/3vk9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3vk9 ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q60GK5_BOMMO Q60GK5_BOMMO]
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BACKGROUND: Glutathione transferase (GST) catalyzes glutathione conjugation, a major detoxification pathway for xenobiotics and endogenous substances. Here, we determined the crystal structure of a Delta-class GST from Bombyx mori (bmGSTD) to examine its catalytic residues. METHODS: The three-dimensional structure of bmGSTD was resolved by the molecular replacement method and refined to a resolution of 2.0A. RESULTS: Structural alignment with a Delta-class GST of Anopheles gambiae indicated that bmGSTD contains 2 distinct domains (an N-terminal domain and a C-terminal domain) connected by a linker. The bound glutathione localized at the N-terminal domain. Putative catalytic residues were changed to alanine by site-directed mutagenesis, and the resulting mutants were characterized in terms of catalytic activity using glutathione and 1-chloro-2,4-dinitrobenzene, a synthetic substrate of GST. Kinetic analysis of bmGSTD mutants indicated that Ser11, Gln51, His52, Ser67, and Arg68 are important for enzyme function. GENERAL SIGNIFICANCE: These results provide structural insights into the catalysis of glutathione conjugation in B. mori by bmGSTD.
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Structural basis for catalytic activity of a silkworm Delta-class glutathione transferase.,Yamamoto K, Usuda K, Kakuta Y, Kimura M, Higashiura A, Nakagawa A, Aso Y, Suzuki M Biochim Biophys Acta. 2012 Oct;1820(10):1469-74. Epub 2012 May 8. PMID:22579926<ref>PMID:22579926</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3vk9" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Glutathione S-transferase|Glutathione S-transferase]]
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*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bommo]]
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[[Category: Bombyx mori]]
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[[Category: Glutathione transferase]]
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[[Category: Large Structures]]
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[[Category: Higashiura, A]]
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[[Category: Higashiura A]]
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[[Category: Kakuta, Y]]
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[[Category: Kakuta Y]]
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[[Category: Kimura, M]]
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[[Category: Kimura M]]
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[[Category: Nakagawa, A]]
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[[Category: Nakagawa A]]
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[[Category: Suzuki, M]]
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[[Category: Suzuki M]]
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[[Category: Usuda, K]]
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[[Category: Usuda K]]
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[[Category: Yamamoto, K]]
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[[Category: Yamamoto K]]
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[[Category: Glutathione binding]]
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[[Category: Transferase]]
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Current revision

Crystal structure of delta-class glutathione transferase from silkmoth

PDB ID 3vk9

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