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 (cyan) and subunit C (magenta) (PDB entry [[3c5w]])' scene='48/489289/Cv/1'>
<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 ==
== 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 />
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== Structural highlights ==
== Structural highlights ==
*<scene name='48/489289/Cv/2'>Human protein phosphatase methylesterase with protein phosphatase 2A subunits A and C</scene>.
*<scene name='48/489289/Cv/6'>Human protein phosphatase methylesterase with protein phosphatase 2A subunits A and C</scene>.
*<scene name='48/489289/Cv/4'>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>.
*<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>.
</StructureSection>


==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]]

Latest revision as of 13:21, 30 October 2019


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.

  • CheB ME is a phosphorylation-activated response regulator involved in reversible modification of bacterial chemotaxis receptors[1]. See Chemotaxis protein.
  • Pectin ME causes demethylation of cell wall polygalactorunanas. It is involved in pectin digestion. The reaction products liberate frothing agents causing bloating in cattle[2].
  • Aclacinomycin ME modifies the aklavinone skeleton in the biosynthesis of anthracyclins in Streptomyces species[3].
  • Protein phosphatase ME is involved in the reversible methylation of protein phosphatase 2A which is active in cellular regulation[4].
  • 4-o-methyl-glucuronoyl ME has a significant role in biomass degradation[5].

Structural highlights

  • .
  • . It inactivates phospholipase 2A by interacting with the latter's subunit C by removing two catalytic Mn+2 ions from it[6].

3D structures of methylesterase

Methylesterase 3D structures


Human protein phosphatase methylesterase (green) complex with protein phosphatase 2A subunit A (cyan) and subunit C (magenta) (PDB entry 3c5w)

Drag the structure with the mouse to rotate

ReferencesReferences

  1. ↑ Simms SA, Keane MG, Stock J. Multiple forms of the CheB methylesterase in bacterial chemosensing. J Biol Chem. 1985 Aug 25;260(18):10161-8. PMID:2991277
  2. ↑ Micheli F. Pectin methylesterases: cell wall enzymes with important roles in plant physiology. Trends Plant Sci. 2001 Sep;6(9):414-9. PMID:11544130
  3. ↑ Wang Y, Niemi J, Mantsala P. Modification of aklavinone and aclacinomycins in vitro and in vivo by rhodomycin biosynthesis gene products. FEMS Microbiol Lett. 2002 Feb 19;208(1):117-22. PMID:11934504
  4. ↑ Wandzioch E, Pusey M, Werda A, Bail S, Bhaskar A, Nestor M, Yang JJ, Rice LM. PME-1 modulates protein phosphatase 2A activity to promote the malignant phenotype of endometrial cancer cells. Cancer Res. 2014 Aug 15;74(16):4295-305. doi: 10.1158/0008-5472.CAN-13-3130. Epub, 2014 Jun 13. PMID:24928782 doi:http://dx.doi.org/10.1158/0008-5472.CAN-13-3130
  5. ↑ Spanikova S, Biely P. Glucuronoyl esterase--novel carbohydrate esterase produced by Schizophyllum commune. FEBS Lett. 2006 Aug 21;580(19):4597-601. Epub 2006 Jul 21. PMID:16876163 doi:http://dx.doi.org/10.1016/j.febslet.2006.07.033
  6. ↑ Xing Y, Li Z, Chen Y, Stock JB, Jeffrey PD, Shi Y. Structural mechanism of demethylation and inactivation of protein phosphatase 2A. Cell. 2008 Apr 4;133(1):154-63. PMID:18394995 doi:http://dx.doi.org/10.1016/j.cell.2008.02.041

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Michal Harel, Alexander Berchansky
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