1p0y

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{{Seed}}
 
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[[Image:1p0y.png|left|200px]]
 
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==Crystal structure of the SET domain of LSMT bound to MeLysine and AdoHcy==
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The line below this paragraph, containing "STRUCTURE_1p0y", creates the "Structure Box" on the page.
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<StructureSection load='1p0y' size='340' side='right'caption='[[1p0y]], [[Resolution|resolution]] 2.55&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'>[[1p0y]] 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=1P0Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P0Y 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]] 2.55&#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=MLZ:N-METHYL-LYSINE'>MLZ</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
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{{STRUCTURE_1p0y| PDB=1p0y | 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=1p0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p0y OCA], [https://pdbe.org/1p0y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p0y RCSB], [https://www.ebi.ac.uk/pdbsum/1p0y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p0y 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/p0/1p0y_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=1p0y ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Crystal structure of the SET domain of LSMT bound to MeLysine and AdoHcy===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1p0y" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_12819771}}, adds the Publication Abstract to the page
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*[[RuBisCO 3D structures|RuBisCO 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 12819771 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12819771}}
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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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1P0Y 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=1P0Y OCA].
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==Reference==
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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]
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[[Category: Pisum sativum]]
[[Category: Pisum sativum]]
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[[Category: Single protein]]
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[[Category: Flynn EM]]
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[[Category: Flynn, E M.]]
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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: Multiple 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 Mon Jul 28 11:52:41 2008''
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Current revision

Crystal structure of the SET domain of LSMT bound to MeLysine and AdoHcy

PDB ID 1p0y

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