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==STRUCTURE OF PYROCOCCUS HORIKOSHII SAM HYDROXIDE ADENOSYLTRANSFERASE IN COMPLEX WITH SAH==
==Structure of Pyrococcus horikoshii SAM hydroxide adenosyltransferase in complex with SAH==
<StructureSection load='2wr8' size='340' side='right' caption='[[2wr8]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
<StructureSection load='2wr8' size='340' side='right'caption='[[2wr8]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2wr8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrho Pyrho]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WR8 FirstGlance]. <br>
<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.77&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1wu8|1wu8]]</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>
<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=2wr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wr8 OCA], [http://pdbe.org/2wr8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wr8 RCSB], [http://www.ebi.ac.uk/pdbsum/2wr8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wr8 ProSAT]</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=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>
</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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wr/2wr8_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wr/2wr8_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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=2wr8 ConSurf].
</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].
<div style="clear:both"></div>
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Pyrho]]
[[Category: Large Structures]]
[[Category: Deng, H]]
[[Category: Pyrococcus horikoshii OT3]]
[[Category: Hagan, D O]]
[[Category: Deng H]]
[[Category: Johnson, K A]]
[[Category: Johnson KA]]
[[Category: Mcmahon, S A]]
[[Category: McMahon SA]]
[[Category: Naismith, J H]]
[[Category: Naismith JH]]
[[Category: Sam]]
[[Category: O'Hagan D]]
[[Category: Sn2]]
[[Category: Transferase]]
[[Category: Water activation]]

Latest revision as of 08:31, 11 December 2025

Structure of Pyrococcus horikoshii SAM hydroxide adenosyltransferase in complex with SAH

2wr8, resolution 1.77Å

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