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Convergent evolution sheds light on the anti-beta-elimination mechanism common to family 1 and 10 polysaccharide lyases

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Published copy (DOI)

Author(s)

  • S J Charnock
  • I E Brown
  • J P Turkenburg
  • G W Black
  • G J Davies

Department/unit(s)

Publication details

JournalProceedings of the National Academy of Sciences of the United States of America
DatePublished - 17 Sep 2002
Issue number19
Volume99
Number of pages6
Pages (from-to)12067-12072
Original languageEnglish

Abstract

Enzyme-catalyzed beta-elimination of sugar uronic acids, exemplified by the degradation of plant cell wall pectins, plays an important role in a wide spectrum of biological processes ranging from the recycling of plant biomass through to pathogen virulence. The three-dimensional crystal structure of the catalytic module of a "family PL-10" polysaccharide lyase, Pel10Acm from Cellvibrio japonicus, solved at a resolution of 1.3 Angstrom, reveals a new polysaccharide lyase fold and is the first example of a polygalacturonic acid lyase that does not exhibit the "parallel beta-helix" topology. The "Michaelis" complex of an inactive mutant in association with the substrate trigalacturonate/Ca2+ reveals the catalytic machinery harnessed by this polygalacturonate lyase, which displays a stunning resemblance, presumably through convergent evolution, to the tetragalacturonic acid complex observed for a structurally unrelated polygalacturonate lyase from family PL-1. Common coordination of the -1 and +1 subsite saccharide carboxylate groups by a protein-liganded Ca2+ ion, the positioning of an arginine catalytic base in close proximity to the a-carbon hydrogen and numerous other conserved enzyme-substrate interactions, considered in light of mutagenesis data for both families, suggest a generic polysaccharicle anti-beta-elimination mechanism.

    Research areas

  • CARBOHYDRATE-ACTIVE ENZYMES, PECTATE LYASE, PSEUDOMONAS-CELLULOSA, 3-DIMENSIONAL STRUCTURE, ERWINIA-CHRYSANTHEMI, CARBOXYLIC-ACIDS, ALPHA-PROTONS, BINDING, SITE, INTERMEDIATE

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