3lbf

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{{STRUCTURE_3lbf| PDB=3lbf | SCENE= }}
 
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===Crystal structure of Protein L-isoaspartyl methyltransferase from Escherichia coli===
 
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==Function==
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==Crystal structure of Protein L-isoaspartyl methyltransferase from Escherichia coli==
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[[http://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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<StructureSection load='3lbf' size='340' side='right'caption='[[3lbf]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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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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</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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<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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==About this Structure==
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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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[[3lbf]] is a 4 chain structure with sequence 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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[[Category: Escherichia coli]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Fang, P.]]
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</div>
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[[Category: Li, X.]]
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<div class="pdbe-citations 3lbf" style="background-color:#fffaf0;"></div>
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[[Category: Niu, L.]]
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== References ==
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[[Category: Teng, M.]]
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<references/>
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[[Category: Wang, J.]]
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__TOC__
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[[Category: Methyltransferase]]
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</StructureSection>
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[[Category: Modified rossman-type fold]]
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[[Category: Escherichia coli K-12]]
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[[Category: S-adenosyl-l-methionine]]
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[[Category: Large Structures]]
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[[Category: Transferase]]
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[[Category: Fang P]]
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[[Category: Li X]]
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[[Category: Niu L]]
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[[Category: Teng M]]
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[[Category: Wang J]]

Current revision

Crystal structure of Protein L-isoaspartyl methyltransferase from Escherichia coli

PDB ID 3lbf

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