Methylesterase: Difference between revisions

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Michal Harel, Alexander Berchansky

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-{{STRUCTURE_2ntb|  PDB=2ntb  | SIZE=400| SCENE= |right|CAPTION=Pectin methylesterase complex with hexasaccharide, [[2ntb]] }}
+<StructureSection load='3c5w' size='350' side='right' caption='Human protein phosphatase methylesterase (green) complex with protein phosphatase 2A subunit A (cyan) and subunit C (magenta) (PDB entry [[3c5w]])' scene='48/489289/Cv/1'>
-<!--
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-'''Methylesterase''' (ME) removes a methyl group from the Υ-glutamyl methyl esther residues of methyl-accepting chemotaxis proteins.  ME participates in several metabolic pathways.  Protein phosphatase ME is involved in the reversible methylation of protein phosphatase 2A which is active in cellular regulation.  Pectin ME causes demethylation of cell wall polygalactorunanas.  It is involved in pectin digestion.  The reaction products liberate frothing agents causing bloating in cattle.  Aclacinomycin ME modifies the aklavinone skeleton in the biosynthesis of anthracyclins in ''Streptomyces'' species.
-==3D structures of methylesterase==
+__TOC__
+== Function ==
+'''Methylesterase''' (ME) removes a methyl group from the Υ-glutamyl methyl esther residues of methyl-accepting chemotaxis proteins.  ME participates in several metabolic pathways.  <br />
+*  '''CheB ME''' is a phosphorylation-activated response regulator involved in reversible modification of bacterial chemotaxis receptors<ref>PMID:2991277</ref>.  See [[Chemotaxis protein]].<br />
+*  '''Pectin ME''' causes demethylation of cell wall polygalactorunanas.  It is involved in pectin digestion.  The reaction products liberate frothing agents causing bloating in cattle<ref>PMID:11544130</ref>.<br />
+*  '''Aclacinomycin ME''' modifies the aklavinone skeleton in the biosynthesis of anthracyclins in ''Streptomyces'' species<ref>PMID:11934504</ref>.  <br />
+*  '''Protein phosphatase ME''' is involved in the reversible methylation of protein phosphatase 2A which is active in cellular regulation<ref>PMID:24928782</ref>.<br />
+*  '''4-o-methyl-glucuronoyl ME''' has a significant role in biomass degradation<ref>PMID:16876163</ref>.<br />
-'''CheB methylesterase'''
+== Structural highlights ==
+*<scene name='48/489289/Cv/6'>Human protein phosphatase methylesterase with protein phosphatase 2A subunits A and C</scene>.
+*<scene name='48/489289/Cv/5'>Protein phosphatase ME binds to the active site of subunit C of phospholipase 2A</scene>.  It inactivates phospholipase 2A by interacting with the latter's subunit C by removing two catalytic Mn+2 ions from it<ref>PMID:18394995</ref>.
-[[1chd]], [[1a2o]] – ME – ''Salmonella typhimurium''<br />
+==3D structures of methylesterase==
-[[3sft]] – TmME catalytic domain – ''Thermotoga maritima''<br />
+[[Methylesterase 3D structures]]
-[[3t8y]] – TmME response regulator domain
-'''Pectin methylesterase'''
-[[1qjv]] – EcME – ''Erwinia chrysanthemi''<br />
-[[1gq8]] – ME – carrot<br />
-[[3uw0]] – ME – ''Yersinia enterocolitica''<br />
-[[1xg2]] – ME + protein inhibitor – ''Solanum lycopersicum''<br />
-[[2nsp]], [[2nst]], [[2nt6]], [[2nt9]] – EcME (mutant) + hexasaccharide<br />
-[[2ntp]], [[2ntb]], [[2ntq]] – EcME + hexasaccharide
-'''Aclacinomycin methylesterase'''
-[[1q0r]], [[1q0z]] – ME + product analog – ''Streptomyces purpurascens''
-'''Protein phosphatase methylesterase'''
+</StructureSection>
-[[3c5v]] – hME1 – human<br />
+== References ==
-[[3c5w]] – hME1 + protein phosphatase 2A
+<references/>
+[[Category:Topic Page]]