2nt9: Difference between revisions

Revision as of 19:10, 21 February 2008

Crystal structure of pectin methylesterase D178A mutant in complex with hexasaccharide IV

OverviewOverview

We provide a mechanism for the activity of pectin methylesterase (PME), the enzyme that catalyses the essential first step in bacterial invasion of plant tissues. The complexes formed in the crystal using specifically methylated pectins, together with kinetic measurements of directed mutants, provide clear insights at atomic resolution into the specificity and the processive action of the Erwinia chrysanthemi enzyme. Product complexes provide additional snapshots along the reaction coordinate. We previously revealed that PME is a novel aspartic-esterase possessing parallel beta-helix architecture and now show that the two conserved aspartates are the nucleophile and general acid-base in the mechanism, respectively. Other conserved residues at the catalytic centre are shown to be essential for substrate binding or transition state stabilisation. The preferential binding of methylated sugar residues upstream of the catalytic site, and demethylated residues downstream, drives the enzyme along the pectin molecule and accounts for the sequential pattern of demethylation produced by both bacterial and plant PMEs.

About this StructureAbout this Structure

2NT9 is a Single protein structure of sequence from Erwinia chrysanthemi. Active as Pectinesterase, with EC number 3.1.1.11 Full crystallographic information is available from OCA.

ReferenceReference

Molecular basis of the activity of the phytopathogen pectin methylesterase., Fries M, Ihrig J, Brocklehurst K, Shevchik VE, Pickersgill RW, EMBO J. 2007 Sep 5;26(17):3879-87. Epub 2007 Aug 23. PMID:17717531

Page seeded by OCA on Thu Feb 21 18:10:47 2008

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OCA

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 ==Overview==
-We provide a mechanism for the activity of pectin methylesterase (PME), the enzyme that catalyses the essential first step in bacterial invasion, of plant tissues. The complexes formed in the crystal using specifically, methylated pectins, together with kinetic measurements of directed, mutants, provide clear insights at atomic resolution into the specificity, and the processive action of the Erwinia chrysanthemi enzyme. Product, complexes provide additional snapshots along the reaction coordinate. We, previously revealed that PME is a novel aspartic-esterase possessing, parallel beta-helix architecture and now show that the two conserved, aspartates are the nucleophile and general acid-base in the mechanism, respectively. Other conserved residues at the catalytic centre are shown, to be essential for substrate binding or transition state stabilisation., The preferential binding of methylated sugar residues upstream of the, catalytic site, and demethylated residues downstream, drives the enzyme, along the pectin molecule and accounts for the sequential pattern of, demethylation produced by both bacterial and plant PMEs.
+We provide a mechanism for the activity of pectin methylesterase (PME), the enzyme that catalyses the essential first step in bacterial invasion of plant tissues. The complexes formed in the crystal using specifically methylated pectins, together with kinetic measurements of directed mutants, provide clear insights at atomic resolution into the specificity and the processive action of the Erwinia chrysanthemi enzyme. Product complexes provide additional snapshots along the reaction coordinate. We previously revealed that PME is a novel aspartic-esterase possessing parallel beta-helix architecture and now show that the two conserved aspartates are the nucleophile and general acid-base in the mechanism, respectively. Other conserved residues at the catalytic centre are shown to be essential for substrate binding or transition state stabilisation. The preferential binding of methylated sugar residues upstream of the catalytic site, and demethylated residues downstream, drives the enzyme along the pectin molecule and accounts for the sequential pattern of demethylation produced by both bacterial and plant PMEs.
 ==About this Structure==
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 [[Category: Brocklehurst, K.]]
 [[Category: Fries, M.]]
-[[Category: Pickersgill, R.W.]]
+[[Category: Pickersgill, R W.]]
-[[Category: Shevchik, V.E.]]
+[[Category: Shevchik, V E.]]
 [[Category: hydrolase]]
 [[Category: michaelis complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:34:19 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:10:47 2008''