Methylesterase: Difference between revisions

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<StructureSection load='3c5w' size='350' side='right' caption='Human protein phosphatase methylesterase (green) complex with protein phosphatase 2A subunit A (grey) and subunit C (pink) (PDB entry [[3c5w]])' scene=''>
<StructureSection load='3c5w' size='350' side='right' caption='Human α-defensin 1 (PDB entry [[2pm4]])' scene=''>
== 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 />
'''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 />
*  '''CheB ME''' is a phosphorylation-activated response regulator involved in reversible modification of bacterial chemotaxis receptors<ref>PMID:2991277</ref>.  See [[Chemotaxis protein]].<br />
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*  '''Protein phosphatase ME''' is involved in the reversible methylation of protein phosphatase 2A which is active in cellular regulation<ref>PMID:24928782</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 />
*  '''4-o-methyl-glucuronoyl ME''' has a significant role in biomass degradation<ref>PMID:16876163</ref>.<br />
== Structural highlights ==
Protein phosphatase ME binds to the active site of subunit C of phospholipase 2A.  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>.
</StructureSection>


==3D structures of methylesterase==
==3D structures of methylesterase==

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Michal Harel, Alexander Berchansky