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2zwa
From Proteopedia
(Difference between revisions)
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==Crystal structure of tRNA wybutosine synthesizing enzyme TYW4== | ==Crystal structure of tRNA wybutosine synthesizing enzyme TYW4== | ||
| - | <StructureSection load='2zwa' size='340' side='right' caption='[[2zwa]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='2zwa' size='340' side='right'caption='[[2zwa]], [[Resolution|resolution]] 1.70Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2zwa]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2zwa]] is a 2 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=2ZWA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZWA FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zw8|2zw8]], [[2zw9|2zw9]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2zw8|2zw8]], [[2zw9|2zw9]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPM2, TYW4, YOL141W ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPM2, TYW4, YOL141W ([https://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'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2zwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zwa OCA], [https://pdbe.org/2zwa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zwa RCSB], [https://www.ebi.ac.uk/pdbsum/2zwa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zwa ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/TYW4_YEAST TYW4_YEAST]] S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the final 2 independent reactions, methylation of the alpha-carboxy group of wybutosine-72 to form wybutosine-58, and methoxycarbonylation of alpha-amino group of wybutosine-58 through the fixation of CO(2) to complete wybutosine.<ref>PMID:16642040</ref> <ref>PMID:17150819</ref> <ref>PMID:19287006</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Atcc 18824]] | [[Category: Atcc 18824]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Ishitani, R]] | [[Category: Ishitani, R]] | ||
[[Category: Noma, A]] | [[Category: Noma, A]] | ||
Revision as of 17:39, 15 December 2021
Crystal structure of tRNA wybutosine synthesizing enzyme TYW4
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Categories: Atcc 18824 | Large Structures | Ishitani, R | Noma, A | Nureki, O | Suzuki, T | Suzuki, Y | Transferase

