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 | == 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== |