2nt9: Difference between revisions

Revision as of 06:19, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2nt9.png

Template:STRUCTURE 2nt9

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

Template:ABSTRACT PUBMED 17717531

About this StructureAbout this Structure

2NT9 is a Single protein structure of sequence from Erwinia chrysanthemi. 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

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

OCA

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-'''Crystal structure of pectin methylesterase D178A mutant in complex with hexasaccharide IV'''
+===Crystal structure of pectin methylesterase D178A mutant in complex with hexasaccharide IV===
-==Overview==
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-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.
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 [[Category: Hydrolase]]
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