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

• Published in: Science (American Association for the Advancement of Science) Vol. 260; no. 5113; pp. 1503 - 1507
• Main Authors: Yoder, M.D, Keen, N.T, Jurnak, F
• Format: Journal Article
• Language: English
• Published: Washington, DC American Society for the Advancement of Science 04.06.1993; American Association for the Advancement of Science
• Subjects: Amino Acid Sequence; Amino acids; Atoms; Bacteriology; Binding Sites; Biological and medical sciences; Calcium; Crystallography; Cylinders; Enzymes; ERWINIA CHRYSANTHEMI; Fundamental and applied biological sciences. Psychology; Hydrogen bonds; Isoenzymes - chemistry; Lead; LIASAS; LYASE; Metabolism. Enzymes; Microbiology; Models, Molecular; Molecular Sequence Data; Oxygen; Pectobacterium chrysanthemi - enzymology; Plants; PODER PATOGENO; Polysaccharide-Lyases - chemistry; POUVOIR PATHOGENE; Protein folding; Protein Structure, Secondary; Protein Structure, Tertiary; Secretion; Virulence (Microbiology); Pectate lyase; Plant pathogen; Enzyme; Erwinia chrysanthemi; Bacteria; Helical structure; β-Structure; Spatial structure; Enterobacteriaceae
• ISSN: 0036-8075; 1095-9203
• 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