2h23

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[[Image:2h23.gif|left|200px]]
 
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==Structure of Rubisco LSMT bound to Trimethyllysine and AdoHcy==
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The line below this paragraph, containing "STRUCTURE_2h23", creates the "Structure Box" on the page.
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<StructureSection load='2h23' size='340' side='right'caption='[[2h23]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2h23]] 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=2H23 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H23 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
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{{STRUCTURE_2h23| PDB=2h23 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2h23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h23 OCA], [https://pdbe.org/2h23 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h23 RCSB], [https://www.ebi.ac.uk/pdbsum/2h23 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h23 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h2/2h23_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2h23 ConSurf].
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<div style="clear:both"></div>
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'''Structure of Rubisco LSMT bound to Trimethyllysine and AdoHcy'''
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==See Also==
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*[[RuBisCO 3D structures|RuBisCO 3D structures]]
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== References ==
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==Overview==
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<references/>
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SET domain enzymes represent a distinct family of protein lysine methyltransferases in eukaryotes. Recent studies have yielded significant insights into the structural basis of substrate recognition and the product specificities of these enzymes. However, the mechanism by which SET domain methyltransferases catalyze the transfer of the methyl group from S-adenosyl-L-methionine to the lysine epsilon-amine has remained unresolved. To elucidate this mechanism, we have determined the structures of the plant SET domain enzyme, pea ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit methyltransferase, bound to S-adenosyl-L-methionine, and its non-reactive analogs Aza-adenosyl-L-methionine and Sinefungin, and characterized the binding of these ligands to a homolog of the enzyme. The structural and biochemical data collectively reveal that S-adenosyl-L-methionine is selectively recognized through carbon-oxygen hydrogen bonds between the cofactor's methyl group and an array of structurally conserved oxygens that comprise the methyl transfer pore in the active site. Furthermore, the structure of the enzyme co-crystallized with the product epsilon-N-trimethyllysine reveals a trigonal array of carbon-oxygen interactions between the epsilon-ammonium methyl groups and the oxygens in the pore. Taken together, these results establish a central role for carbon-oxygen hydrogen bonding in aligning the cofactor's methyl group for transfer to the lysine epsilon-amine and in coordinating the methyl groups after transfer to facilitate multiple rounds of lysine methylation.
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2H23 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H23 OCA].
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==Reference==
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Catalytic roles for carbon-oxygen hydrogen bonding in SET domain lysine methyltransferases., Couture JF, Hauk G, Thompson MJ, Blackburn GM, Trievel RC, J Biol Chem. 2006 Jul 14;281(28):19280-7. Epub 2006 May 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16682405 16682405]
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[[Category: Pisum sativum]]
[[Category: Pisum sativum]]
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[[Category: Single protein]]
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[[Category: Couture JF]]
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[[Category: Couture, J F.]]
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[[Category: Hauk G]]
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[[Category: Hauk, G.]]
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[[Category: Trievel RC]]
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[[Category: Trievel, R C.]]
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[[Category: Protein lysine methyltransferase]]
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[[Category: Set domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:46:53 2008''
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Current revision

Structure of Rubisco LSMT bound to Trimethyllysine and AdoHcy

PDB ID 2h23

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