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3g5t
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3g5t is ON HOLD Authors: Description: Crystal Structure of Trans-aconitate 3-methyltransferase from Yeast ''Page seeded by [http://oca.weizmann.a...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of trans-aconitate 3-methyltransferase from yeast== | |
| - | + | <StructureSection load='3g5t' size='340' side='right'caption='[[3g5t]], [[Resolution|resolution]] 1.12Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3g5t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G5T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G5T FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=T8N:(2E)-2-(2-METHOXY-2-OXOETHYL)BUT-2-ENEDIOIC+ACID'>T8N</scene></td></tr> | |
| - | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |
| - | '' | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">P32643, S000000977, SYGP-ORF63, TAM1, TMT1, YER175C ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr> |
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Trans-aconitate_3-methyltransferase Trans-aconitate 3-methyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.145 2.1.1.145] </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=3g5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g5t OCA], [https://pdbe.org/3g5t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g5t RCSB], [https://www.ebi.ac.uk/pdbsum/3g5t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g5t ProSAT], [https://www.topsan.org/Proteins/CESG/3g5t TOPSAN]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/TMT1_YEAST TMT1_YEAST]] Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate and 3-isopropylmalate at high affinity and of other molecules like cis-aconitate, isocitrate, and citrate at lower velocities and affinities. The function of trans-aconitate methylation appears to be in reducing the toxicity of this spontaneous breakdown product of cis-aconitate. The role of 3-isopropylmalate methylation is unclear but may represent a metabolic branch at 3-isopropylmalate, where some of the material is taken in the pathway leading to leucine and some is taken in a pathway to the 3-isopropylmalate methyl ester, a molecule that provides a signal to switch from vegetative to invasive growth in response to amino acid starvation.<ref>PMID:11695919</ref> <ref>PMID:15147181</ref> <ref>PMID:18092814</ref> | ||
| + | == 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/g5/3g5t_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=3g5t ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Atcc 18824]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Trans-aconitate 3-methyltransferase]] | ||
| + | [[Category: Bingman, C A]] | ||
| + | [[Category: Burgie, E S]] | ||
| + | [[Category: Structural genomic]] | ||
| + | [[Category: Phillips, G N]] | ||
| + | [[Category: Wesenberg, G E]] | ||
| + | [[Category: Cesg]] | ||
| + | [[Category: Cytoplasm]] | ||
| + | [[Category: Methyltransferase]] | ||
| + | [[Category: Phosphoprotein]] | ||
| + | [[Category: PSI, Protein structure initiative]] | ||
| + | [[Category: S-adenosyl-l-methionine]] | ||
| + | [[Category: Transferase]] | ||
Current revision
Crystal structure of trans-aconitate 3-methyltransferase from yeast
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