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| | ==Crystal structure of Protein L-isoaspartyl-O-methyltransferase of Vibrio cholerae== | | ==Crystal structure of Protein L-isoaspartyl-O-methyltransferase of Vibrio cholerae== |
| - | <StructureSection load='4l7v' size='340' side='right' caption='[[4l7v]], [[Resolution|resolution]] 2.05Å' scene=''> | + | <StructureSection load='4l7v' size='340' side='right'caption='[[4l7v]], [[Resolution|resolution]] 2.05Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4l7v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibc3 Vibc3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L7V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L7V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4l7v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae_O395 Vibrio cholerae O395]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L7V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L7V FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pcm, VC0395_A0060, VC395_0549 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=345073 VIBC3])</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=4l7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l7v OCA], [https://pdbe.org/4l7v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l7v RCSB], [https://www.ebi.ac.uk/pdbsum/4l7v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l7v ProSAT]</span></td></tr> |
| - | <tr id='activity'><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>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4l7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l7v OCA], [http://pdbe.org/4l7v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4l7v RCSB], [http://www.ebi.ac.uk/pdbsum/4l7v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4l7v ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PIMT_VIBC3 PIMT_VIBC3]] 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 (By similarity). | + | [https://www.uniprot.org/uniprot/PIMT_VIBC3 PIMT_VIBC3] 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 (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Vibc3]] | + | [[Category: Large Structures]] |
| - | [[Category: Chakrabarti, P]] | + | [[Category: Vibrio cholerae O395]] |
| - | [[Category: Chatterjee, T]] | + | [[Category: Chakrabarti P]] |
| - | [[Category: Mukherjee, D]] | + | [[Category: Chatterjee T]] |
| - | [[Category: Isoaspartyl peptide]] | + | [[Category: Mukherjee D]] |
| - | [[Category: Protein repair]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
PIMT_VIBC3 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 (By similarity).
Publication Abstract from PubMed
The repair enzyme Protein L-isoaspartyl-O-methyltransferase (PIMT) is widely distributed in various organisms. PIMT catalyzes S-adenosylmethionine (AdoMet) dependent methylation of abnormal L-isoaspartyl residues, formed by the deamidation of asparagines and isomerization of aspartates. We report the crystal structure of PIMT of Vibrio cholerae (VcPIMT), the aetiological agent for cholera, complexed with the demethylated cofactor S-adenosyl-L-homocysteine (AdoHcy) to 2.05 A resolution. A stretch of residues (39-58), lining the substrate-binding site, is disordered. Urea-induced unfolding free energy for apo and VcPIMT-AdoHcy complex reveals greater stability for the cofactor-bound protein. The kinetic parameters for the methyltransferase activity of the recombinant VcPIMT was determined using a continuous spectrophotometric color-based assay using the peptide substrate [VYP(L-isoD)HA]. The enzyme exhibited activity higher than the Escherichia coli enzyme and closer to those from thermophilic bacteria and the mammalian source. The association constant for substrate binding is 2.29 x 10(6) M(-1), quite similar to that for AdoHcy. The crystal structure and the model of the peptide-bound structure indicate that the majority of the interactions used for cofactor/substrate binding are provided by the main-chain atoms. Evolutionary relationships derived based on a phylogenetic tree constructed using the PIMT sequences are in conformity with the crystal structures of nine AdoHcy-bound PIMTs.
Crystal structure and activity of protein L-isoaspartyl-O-methyltransferase from Vibrio cholerae, and the effect of AdoHcy binding.,Chatterjee T, Mukherjee D, Banerjee M, Chatterjee BK, Chakrabarti P Arch Biochem Biophys. 2015 Oct 1;583:140-9. doi: 10.1016/j.abb.2015.08.001. Epub , 2015 Aug 6. PMID:26255776[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chatterjee T, Mukherjee D, Banerjee M, Chatterjee BK, Chakrabarti P. Crystal structure and activity of protein L-isoaspartyl-O-methyltransferase from Vibrio cholerae, and the effect of AdoHcy binding. Arch Biochem Biophys. 2015 Oct 1;583:140-9. doi: 10.1016/j.abb.2015.08.001. Epub , 2015 Aug 6. PMID:26255776 doi:http://dx.doi.org/10.1016/j.abb.2015.08.001
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