3lbf

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{{Seed}}
 
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[[Image:3lbf.jpg|left|200px]]
 
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==Crystal structure of Protein L-isoaspartyl methyltransferase from Escherichia coli==
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The line below this paragraph, containing "STRUCTURE_3lbf", creates the "Structure Box" on the page.
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<StructureSection load='3lbf' size='340' side='right'caption='[[3lbf]], [[Resolution|resolution]] 1.80&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'>[[3lbf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LBF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LBF 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]] 1.8&#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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
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{{STRUCTURE_3lbf| PDB=3lbf | 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=3lbf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lbf OCA], [https://pdbe.org/3lbf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lbf RCSB], [https://www.ebi.ac.uk/pdbsum/3lbf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lbf ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PIMT_ECOLI PIMT_ECOLI] Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins. This enzyme does not act on D-aspartyl residues.[HAMAP-Rule:MF_00090]
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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/lb/3lbf_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=3lbf 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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Among the known covalent damages that can occur spontaneously to proteins, the formation of isoaspartyl linkages through deamidation of asparagines and isomerization of aspartates may be one of the most rapid forms under conditions of physiological pH and temperature. The protein L-isoaspartyl methyltransferase (PIMT) is thought to recognize L-isoaspartyl residues and repair this kind of damaged proteins. Curiously, there is a potential functional difference between bacterial and mammalian PIMTs. Herein, we present the crystal structure of Escherichia coli PIMT (EcPIMT) at a resolution of 1.8 A. The enzyme we investigated was able to remain bound to its product S-adenosylhomocysteine (SAH) during crystallization. Analysis indicates that the high affinity of EcPIMT for SAH might lead to the lower activity of the enzyme.
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===Crystal structure of Protein L-isoaspartyl methyltransferase from Escherichia coli===
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Crystal structure of the protein L-isoaspartyl methyltransferase from Escherichia coli.,Fang P, Li X, Wang J, Xing L, Gao Y, Niu L, Teng M Cell Biochem Biophys. 2010 Dec;58(3):163-7. doi: 10.1007/s12013-010-9103-2. PMID:20857228<ref>PMID:20857228</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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==About this Structure==
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</div>
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3LBF is a 4 chains structure with sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LBF OCA].
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<div class="pdbe-citations 3lbf" style="background-color:#fffaf0;"></div>
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[[Category: Escherichia coli]]
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== References ==
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[[Category: Fang, P.]]
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<references/>
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[[Category: Li, X.]]
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__TOC__
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[[Category: Niu, L.]]
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</StructureSection>
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[[Category: Teng, M.]]
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[[Category: Escherichia coli K-12]]
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[[Category: Wang, J.]]
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[[Category: Large Structures]]
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[[Category: Methyltransferase]]
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[[Category: Fang P]]
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[[Category: Modified rossman-type fold]]
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[[Category: Li X]]
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[[Category: S-adenosyl-l-methionine]]
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[[Category: Niu L]]
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[[Category: Transferase]]
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[[Category: Teng M]]
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[[Category: Wang J]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Sep 10 13:57:45 2010''
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Current revision

Crystal structure of Protein L-isoaspartyl methyltransferase from Escherichia coli

PDB ID 3lbf

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