1mlv

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[[Image:1mlv.gif|left|200px]]
 
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==Structure and Catalytic Mechanism of a SET Domain Protein Methyltransferase==
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The line below this paragraph, containing "STRUCTURE_1mlv", creates the "Structure Box" on the page.
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<StructureSection load='1mlv' size='340' side='right'caption='[[1mlv]], [[Resolution|resolution]] 2.60&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'>[[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>
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or leave the SCENE parameter empty for the default display.
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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]] 2.6&#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=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
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{{STRUCTURE_1mlv| PDB=1mlv | 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=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>
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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/ml/1mlv_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=1mlv ConSurf].
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<div style="clear:both"></div>
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'''Structure and Catalytic Mechanism of a SET Domain Protein Methyltransferase'''
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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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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.
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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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1MLV 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=1MLV OCA].
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/12372303 12372303]
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[[Category: Pisum sativum]]
[[Category: Pisum sativum]]
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[[Category: Single protein]]
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[[Category: Beach BM]]
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[[Category: Beach, B M.]]
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[[Category: Dirk LMA]]
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[[Category: Dirk, L M.A.]]
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[[Category: Houtz RL]]
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[[Category: Houtz, R L.]]
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[[Category: Hurley JH]]
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[[Category: Hurley, J H.]]
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[[Category: Trievel RC]]
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[[Category: Trievel, R C.]]
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[[Category: Lysine n-methylation]]
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[[Category: Photosynthesis]]
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[[Category: Post-translational modification]]
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[[Category: Set domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:23:49 2008''
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Current revision

Structure and Catalytic Mechanism of a SET Domain Protein Methyltransferase

PDB ID 1mlv

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