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3lbf

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==Crystal structure of Protein L-isoaspartyl methyltransferase from Escherichia coli==
==Crystal structure of Protein L-isoaspartyl methyltransferase from Escherichia coli==
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<StructureSection load='3lbf' size='340' side='right' caption='[[3lbf]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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<StructureSection load='3lbf' size='340' side='right'caption='[[3lbf]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3lbf]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LBF FirstGlance]. <br>
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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><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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><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><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-L-isoaspartate(D-aspartate)_O-methyltransferase Protein-L-isoaspartate(D-aspartate) O-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.77 2.1.1.77] </span></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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3lbf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lbf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lbf RCSB], [http://www.ebi.ac.uk/pdbsum/3lbf PDBsum]</span></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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</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]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<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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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lb/3lbf_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
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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].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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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>
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®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 3lbf" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ecoli]]
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[[Category: Escherichia coli K-12]]
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[[Category: Fang, P.]]
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[[Category: Large Structures]]
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[[Category: Li, X.]]
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[[Category: Fang P]]
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[[Category: Niu, L.]]
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[[Category: Li X]]
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[[Category: Teng, M.]]
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[[Category: Niu L]]
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[[Category: Wang, J.]]
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[[Category: Teng M]]
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[[Category: Methyltransferase]]
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[[Category: Wang J]]
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[[Category: Modified rossman-type fold]]
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[[Category: S-adenosyl-l-methionine]]
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[[Category: Transferase]]
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Current revision

Crystal structure of Protein L-isoaspartyl methyltransferase from Escherichia coli

PDB ID 3lbf

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