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4o89
From Proteopedia
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<StructureSection load='4o89' size='340' side='right'caption='[[4o89]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='4o89' size='340' side='right'caption='[[4o89]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4o89]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[4o89]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O89 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O89 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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></td></tr> | |
| - | <tr id=' | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4o89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o89 OCA], [https://pdbe.org/4o89 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o89 RCSB], [https://www.ebi.ac.uk/pdbsum/4o89 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o89 ProSAT]</span></td></tr> |
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/RTCA_PYRHO RTCA_PYRHO] Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing (By similarity). |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Pyrococcus horikoshii | + | [[Category: Pyrococcus horikoshii OT3]] |
| - | + | [[Category: Bingman CA]] | |
| - | [[Category: Bingman | + | [[Category: Desai KK]] |
| - | [[Category: Desai | + | [[Category: Phillips Jr GN]] |
| - | [[Category: Jr | + | [[Category: Raines RT]] |
| - | [[Category: Raines | + | |
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Current revision
Crystal structure of RtcA, the RNA 3'-terminal phosphate cyclase from Pyrococcus horikoshii.
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