1mlv

<StructureSection load='1mlv' size='340' side='right' caption='[[1mlv]], [[Resolution|resolution]] 2.60&Aring;' scene=''>

<table><tr><td colspan='2'>[[1mlv]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Garden_pea Garden pea]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MLV FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></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=1mlv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mlv OCA], [http://pdbe.org/1mlv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mlv RCSB], [http://www.ebi.ac.uk/pdbsum/1mlv PDBsum]</span></td></tr>

[[http://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>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ml/1mlv_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

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.

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:12372303<ref>PMID:12372303</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1mlv" style="background-color:#fffaf0;"></div>

*[[RuBisCO|RuBisCO]]

[[Category: Garden pea]]

[[Category: Beach, B M]]

[[Category: Dirk, L M.A]]

[[Category: Houtz, R L]]

[[Category: Hurley, J H]]

[[Category: Trievel, R C]]

[[Category: Lysine n-methylation]]

[[Category: Transferase]]