title: Structure-based multiple alignment of extracellular pectate lyase sequences.
abstract: Pectate lyases are secreted virulence factors which degrade the pectate component of plant cell walls. The evolutionary-based multiple alignment of extracellular pectate lyases has been corrected using three-dimensional structural information derived from Erwinia chyrsanthemi pectate lyases C and E. The new multiple alignment reveals invariant amino acids likely to be involved in two different enzymatic functions.
authors.affiliation: Department of Biochemistry, University of California, Riverside 92521, USA.
authors.forename: S
authors.initials: S
authors.lastname: Heffron
authors.forename: B
authors.initials: B
authors.lastname: Henrissat
authors.forename: M D
authors.initials: MD
authors.lastname: Yoder
authors.forename: S
authors.initials: S
authors.lastname: Lietzke
authors.forename: F
authors.initials: F
authors.lastname: Jurnak
mesh_terms: D000595:Amino Acid Sequence; D016974:Dickeya chrysanthemi / Q000201:enzymology; D007527:Isoenzymes / Q000737:chemistry* / Q000235:genetics; D008969:Molecular Sequence Data; D011133:Polysaccharide-Lyases / Q000737:chemistry* / Q000235:genetics; D017386:Sequence Homology, Amino Acid
chemical_list: D007527:Isoenzymes; D011133:Polysaccharide-Lyases; C023911:pectate lyase