Structure-based multiple alignment of extracellular pectate lyase sequences.

S Heffron; B Henrissat; M D Yoder; S Lietzke; F Jurnak

doi:10.1094/mpmi-8-0331

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Structure-based multiple alignment of extracellular pectate lyase sequences.

S Heffron·B Henrissat·M D Yoder·S Lietzke·F Jurnak

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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.

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Amino Acid Sequence Dickeya chrysanthemi Isoenzymes Molecular Sequence Data Polysaccharide-Lyases Sequence Homology, Amino Acid Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

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S Heffron, B Henrissat, M D Yoder, S Lietzke, F Jurnak. Structure-based multiple alignment of extracellular pectate lyase sequences.. https://doi.org/10.1094/mpmi-8-0331

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