New domain motif: the structure of pectate lyase C, a secreted plant virulence factor.
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.
Department of Biochemistry, University of California, Riverside 92521.
M D
MD
Yoder
N T
NT
Keen
F
F
Jurnak
D000595:Amino Acid Sequence; D001665:Binding Sites; D002118:Calcium; D003461:Crystallography; D016974:Dickeya chrysanthemi / Q000201:enzymology; D007527:Isoenzymes / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011133:Polysaccharide-Lyases / Q000737:chemistry*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
D007527:Isoenzymes; D011133:Polysaccharide-Lyases; C023911:pectate lyase; D002118:Calcium