2wr8
From Proteopedia
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| - | [[Image:2wr8.png|left|200px]] | ||
| - | + | ==Structure of Pyrococcus horikoshii SAM hydroxide adenosyltransferase in complex with SAH== | |
| - | + | <StructureSection load='2wr8' size='340' side='right'caption='[[2wr8]], [[Resolution|resolution]] 1.77Å' scene=''> | |
| - | === | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[2wr8]] is a 1 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=2WR8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WR8 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.77Å</td></tr> | |
| - | == | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> |
| - | [[2wr8]] is a 1 chain structure with sequence from [ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2wr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wr8 OCA], [https://pdbe.org/2wr8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wr8 RCSB], [https://www.ebi.ac.uk/pdbsum/2wr8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wr8 ProSAT]</span></td></tr> |
| - | + | </table> | |
| - | == | + | == Function == |
| - | < | + | [https://www.uniprot.org/uniprot/RSAMH_PYRHO RSAMH_PYRHO] Catalyzes the hydrolysis of S-adenosyl-L-methionine (SAM) into adenosine and L-methionine (PubMed:18551689). Is likely stereoselective, specifically hydrolyzing (R)-S-adenosyl-L-methionine ((R)-SAM), the inactive form of the ubiquitous cofactor SAM, and not the active form of SAM, (S)-S-adenosyl-L-methionine (By similarity). Probaly plays a role in preventing accumulation of (R)-S-adenosyl-L-methionine in cells; maintenance of (S)-S-denosyl-L-methionine homochirality is important for cellular health given that the (R)-form is largely inactive as a methyl donor and can function as an inhibitor of methyltransferases (By similarity). Is unable to mediate a fluorination or chlorination reaction with SAM (PubMed:18551689).[UniProtKB:A4X4S2]<ref>PMID:18551689</ref> |
| - | [[ | + | == Evolutionary Conservation == |
| - | [[ | + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | [[ | + | Check<jmol> |
| - | [[Category: | + | <jmolCheckbox> |
| - | [[Category: | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wr/2wr8_consurf.spt"</scriptWhenChecked> |
| - | [[Category: | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| - | [[Category: | + | <text>to colour the structure by Evolutionary Conservation</text> |
| - | [[Category: | + | </jmolCheckbox> |
| - | [[Category: | + | </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=2wr8 ConSurf]. |
| - | [[Category: | + | <div style="clear:both"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pyrococcus horikoshii OT3]] | ||
| + | [[Category: Deng H]] | ||
| + | [[Category: Johnson KA]] | ||
| + | [[Category: McMahon SA]] | ||
| + | [[Category: Naismith JH]] | ||
| + | [[Category: O'Hagan D]] | ||
Current revision
Structure of Pyrococcus horikoshii SAM hydroxide adenosyltransferase in complex with SAH
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