期刊
EMBO JOURNAL
卷 26, 期 17, 页码 3879-3887出版社
WILEY
DOI: 10.1038/sj.emboj.7601816
关键词
mechanism; pectin methylesterase; processivity; specificity
资金
- Biotechnology and Biological Sciences Research Council [BBS/B/07896] Funding Source: Medline
- Biotechnology and Biological Sciences Research Council [BBS/B/07896] Funding Source: researchfish
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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