Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases.

@article{Mayans1997TwoCS,
  title={Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases.},
  author={Olga Mayans and Moira Scott and Ian Frank Connerton and T N Gravesen and Jaques A. E. Benen and J. Arjan G. M. de Visser and Richard Pickersgill and John M Jenkins},
  journal={Structure},
  year={1997},
  volume={5 5},
  pages={
          677-89
        }
}
BACKGROUND Microbial pectin and pectate lyases are virulence factors that degrade the pectic components of the plant cell wall. The homogalacturan backbone of pectin varies in its degree of methylation from the highly methylated and relatively hydrophobic form known as pectin, to the fully demethylated and highly charged form known as pectate. Methylated and demethylated regions of pectin are cleaved by pectin lyase and calcium-dependent pectate lyases, respectively. Protein engineering of… CONTINUE READING
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