Methylesterase: Difference between revisions

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{{STRUCTURE_3uw0|  PDB=3uw0  | SIZE=400| SCENE= |right|CAPTION=Pectin methylesterase [[3uw0]] }}
<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'>


__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 />
'''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 ==
*<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>.


==3D structures of methylesterase==
==3D structures of methylesterase==
[[Methylesterase 3D structures]]


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
</StructureSection>
{{#tree:id=OrganizedByTopic|openlevels=0|
 
*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
 
**[[3c5v]] – hME1 – human<br />
**[[3c5w]] – hME1 + protein phosphatase 2A
 
*4-o-methyl-glucuronoyl methylesterase
 
**[[4g4g]] – MtME – ''Myceliophthora thermophila''<br />
**[[4g4i]] – MtME (mutant)<br />
**[[4g4j]] – MtME (mutant) + 4-o-methyl-β-D-glucopyranuronate<br />


*CheB methylesterase see [[Chemotaxis protein]]
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky