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New page: left|200px<br /><applet load="1mlv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mlv, resolution 2.60Å" /> '''Structure and Cataly...
 
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[[Image:1mlv.gif|left|200px]]<br /><applet load="1mlv" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1mlv, resolution 2.60&Aring;" />
'''Structure and Catalytic Mechanism of a SET Domain Protein Methyltransferase'''<br />


==Overview==
==Structure and Catalytic Mechanism of a SET Domain Protein Methyltransferase==
Protein lysine methylation by SET domain enzymes regulates chromatin, structure, gene silencing, transcriptional activation, plant metabolism, and other processes. The 2.6 A resolution structure of Rubisco large, subunit methyltransferase in a pseudo-bisubstrate complex with, S-adenosylhomocysteine and a HEPES ion reveals an all-beta architecture, for the SET domain embedded within a larger alpha-helical enzyme fold., Conserved regions of the SET domain bind S-adenosylmethionine and, substrate lysine at two sites connected by a pore. We propose that methyl, transfer is catalyzed by a conserved Tyr at a narrow pore connecting the, sites. The cofactor enters by a "back door" on the opposite side of the, enzyme from substrate, promoting highly specific protein recognition and, allowing addition of multiple methyl groups.
<StructureSection load='1mlv' size='340' side='right'caption='[[1mlv]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1mlv]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MLV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MLV 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]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=1mlv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mlv OCA], [https://pdbe.org/1mlv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mlv RCSB], [https://www.ebi.ac.uk/pdbsum/1mlv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mlv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RBCMT_PEA RBCMT_PEA] Methylates 'Lys-14' of the large subunit of RuBisCO. Can also use with lower efficiency chloroplastic fructose-bisphosphate aldolases and gamma-tocopherol methyltransferase as substrates, but not a cytosolic aldolase.<ref>PMID:22547063</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/ml/1mlv_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=1mlv ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1MLV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] with SAH and EPE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/[Ribulose-bisphosphate_carboxylase]-lysine_N-methyltransferase [Ribulose-bisphosphate carboxylase]-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.127 2.1.1.127] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MLV OCA].
*[[RuBisCO 3D structures|RuBisCO 3D structures]]
 
== References ==
==Reference==
<references/>
Structure and catalytic mechanism of a SET domain protein methyltransferase., Trievel RC, Beach BM, Dirk LM, Houtz RL, Hurley JH, Cell. 2002 Oct 4;111(1):91-103. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12372303 12372303]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pisum sativum]]
[[Category: Pisum sativum]]
[[Category: Single protein]]
[[Category: Beach BM]]
[[Category: [Ribulose-bisphosphate carboxylase]-lysine N-methyltransferase]]
[[Category: Dirk LMA]]
[[Category: Beach, B.M.]]
[[Category: Houtz RL]]
[[Category: Dirk, L.M.A.]]
[[Category: Hurley JH]]
[[Category: Houtz, R.L.]]
[[Category: Trievel RC]]
[[Category: Hurley, J.H.]]
[[Category: Trievel, R.C.]]
[[Category: EPE]]
[[Category: SAH]]
[[Category: lysine n-methylation]]
[[Category: photosynthesis]]
[[Category: post-translational modification]]
[[Category: set domain]]
 
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