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3lbf
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<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> | <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> | ||
| - | </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>< | + | </td></tr><tr id='ligand'><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></td></tr> |
| - | <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> | + | <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><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> | + | <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=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> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[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] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
== References == | == References == | ||
| Line 30: | Line 32: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Ecoli]] | [[Category: Ecoli]] | ||
| - | [[Category: Fang, P | + | [[Category: Fang, P]] |
| - | [[Category: Li, X | + | [[Category: Li, X]] |
| - | [[Category: Niu, L | + | [[Category: Niu, L]] |
| - | [[Category: Teng, M | + | [[Category: Teng, M]] |
| - | [[Category: Wang, J | + | [[Category: Wang, J]] |
[[Category: Methyltransferase]] | [[Category: Methyltransferase]] | ||
[[Category: Modified rossman-type fold]] | [[Category: Modified rossman-type fold]] | ||
[[Category: S-adenosyl-l-methionine]] | [[Category: S-adenosyl-l-methionine]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 22:12, 25 December 2014
Crystal structure of Protein L-isoaspartyl methyltransferase from Escherichia coli
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