New domain motif: the structure of pectate lyase C, a secreted plant virulence factor

Science. 1993 Jun 4;260(5113):1503-7. doi: 10.1126/science.8502994.


Pectate lyases are secreted by pathogens and initiate soft-rot diseases in plants by cleaving polygalacturonate, a major component of the plant cell wall. The three-dimensional structure of pectate lyase C from Erwinia chrysanthemi has been solved and refined to a resolution of 2.2 angstroms. The enzyme folds into a unique motif of parallel beta strands coiled into a large helix. Within the core, the amino acids form linear stacks and include a novel asparagine ladder. The sequence similarities that pectate lyases share with pectin lyases, pollen and style proteins, and tubulins suggest that the parallel beta helix motif may occur in a broad spectrum of proteins.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Calcium
  • Crystallography
  • Dickeya chrysanthemi / enzymology
  • Isoenzymes / chemistry*
  • Models, Molecular
  • Molecular Sequence Data
  • Polysaccharide-Lyases / chemistry*
  • Protein Structure, Secondary
  • Protein Structure, Tertiary*


  • Isoenzymes
  • Polysaccharide-Lyases
  • pectate lyase
  • Calcium