1ozv: Difference between revisions

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-[[Image:1ozv.jpg|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1ozv", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
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-{{STRUCTURE_1ozv|  PDB=1ozv  |  SCENE=  }}
-'''Crystal structure of the SET domain of LSMT bound to Lysine and AdoHcy'''
+==Crystal structure of the SET domain of LSMT bound to Lysine and AdoHcy==
+<StructureSection load='1ozv' size='340' side='right'caption='[[1ozv]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1ozv]] 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=1OZV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OZV 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]] 2.65&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LYS:LYSINE'>LYS</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=1ozv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ozv OCA], [https://pdbe.org/1ozv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ozv RCSB], [https://www.ebi.ac.uk/pdbsum/1ozv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ozv 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/oz/1ozv_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=1ozv ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+SET domain protein methyltransferases catalyze the transfer of methyl groups from the cofactor S-adenosylmethionine (AdoMet) to specific lysine residues of protein substrates, such as the N-terminal tails of histones H3 and H4 and the large subunit of the Rubisco holoenzyme complex. The crystal structures of pea Rubisco large subunit methyltransferase (LSMT) in ternary complexes with either lysine or epsilon-N-methyllysine (MeLys) and the product S-adenosylhomocysteine (AdoHcy) were determined to resolutions of 2.65 and 2.55 A, respectively. The zeta-methyl group of MeLys is bound to the enzyme via carbon-oxygen hydrogen bonds that play a key role in catalysis. The methyl donor and acceptor are aligned in a linear geometry for S(N)2 nucleophilic transfer of the methyl group during catalysis. Differences in hydrogen bonding between the MeLys epsilon-amino group and Rubisco LSMT and SET7/9 explain why Rubisco LSMT generates multiply methylated Lys, wheras SET7/9 generates only MeLys.
-==Overview==
+Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT.,Trievel RC, Flynn EM, Houtz RL, Hurley JH Nat Struct Biol. 2003 Jul;10(7):545-52. PMID:12819771<ref>PMID:12819771</ref>
-SET domain protein methyltransferases catalyze the transfer of methyl groups from the cofactor S-adenosylmethionine (AdoMet) to specific lysine residues of protein substrates, such as the N-terminal tails of histones H3 and H4 and the large subunit of the Rubisco holoenzyme complex. The crystal structures of pea Rubisco large subunit methyltransferase (LSMT) in ternary complexes with either lysine or epsilon-N-methyllysine (MeLys) and the product S-adenosylhomocysteine (AdoHcy) were determined to resolutions of 2.65 and 2.55 A, respectively. The zeta-methyl group of MeLys is bound to the enzyme via carbon-oxygen hydrogen bonds that play a key role in catalysis. The methyl donor and acceptor are aligned in a linear geometry for S(N)2 nucleophilic transfer of the methyl group during catalysis. Differences in hydrogen bonding between the MeLys epsilon-amino group and Rubisco LSMT and SET7/9 explain why Rubisco LSMT generates multiply methylated Lys, wheras SET7/9 generates only MeLys.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-OZV 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=1OZV OCA].
+</div>
+<div class="pdbe-citations 1ozv" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT., Trievel RC, Flynn EM, Houtz RL, Hurley JH, Nat Struct Biol. 2003 Jul;10(7):545-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12819771 12819771]
+*[[RuBisCO 3D structures|RuBisCO 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Pisum sativum]]
-[[Category: Single protein]]
+[[Category: Flynn EM]]
-[[Category: Flynn, E M.]]
+[[Category: Houtz RL]]
-[[Category: Houtz, R L.]]
+[[Category: Hurley JH]]
-[[Category: Hurley, J H.]]
+[[Category: Trievel RC]]
-[[Category: Trievel, R C.]]
-[[Category: Lysine n-methylation]]
-[[Category: Multiple methylation]]
-[[Category: Photosynthesis]]
-[[Category: Post-translational modification]]
-[[Category: Set domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:29:50 2008''