Molecular basis of the activity of the phytopathogen pectin methylesterase
| Autor: | Richard W. Pickersgill, Jessica Ihrig, Markus Fries, Keith Brocklehurst, Vladimir E. Shevchik |
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| Přispěvatelé: | School of Biological and Chemical Sciences, Queen Mary University of London (QMUL), Microbiologie, adaptation et pathogénie (MAP), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Institut National des Sciences Appliquées (INSA)-Université de Lyon-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS), Trafic et signalisation membranaires chez les bactéries (MTSB), Institut National des Sciences Appliquées (INSA)-Université de Lyon-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL) |
| Jazyk: | angličtina |
| Rok vydání: | 2007 |
| Předmět: |
0106 biological sciences
Models Molecular food.ingredient Pectin Protein Conformation [SDV]Life Sciences [q-bio] Plasma protein binding Biology Crystallography X-Ray 01 natural sciences General Biochemistry Genetics and Molecular Biology Catalysis Article Substrate Specificity 03 medical and health sciences food Protein structure Catalytic Domain Hydrolase [CHIM]Chemical Sciences Molecular Biology ComputingMilieux_MISCELLANEOUS 030304 developmental biology Demethylation chemistry.chemical_classification 0303 health sciences General Immunology and Microbiology General Neuroscience Dickeya chrysanthemi Substrate (chemistry) Processivity Enzyme Biochemistry chemistry Mutation Pectins Carboxylic Ester Hydrolases 010606 plant biology & botany Protein Binding |
| Zdroj: | EMBO Journal EMBO Journal, EMBO Press, 2007, 26 (17), pp.3879-3887. ⟨10.1038/sj.emboj.7601816⟩ |
| ISSN: | 0261-4189 1460-2075 |
| DOI: | 10.1038/sj.emboj.7601816⟩ |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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