NEW DOMAIN MOTIF - THE STRUCTURE OF PECTATE LYASE-C, A SECRETED PLANTVIRULENCE FACTOR

Citation
Md. Yoder et al., NEW DOMAIN MOTIF - THE STRUCTURE OF PECTATE LYASE-C, A SECRETED PLANTVIRULENCE FACTOR, Science, 260(5113), 1993, pp. 1503-1507
Citations number
39
Categorie Soggetti
Multidisciplinary Sciences
Journal title
ISSN journal
00368075
Volume
260
Issue
5113
Year of publication
1993
Pages
1503 - 1507
Database
ISI
SICI code
0036-8075(1993)260:5113<1503:NDM-TS>2.0.ZU;2-V
Abstract
Pectate lyases are secreted by pathogens and initiate soft-rot disease s in plants by cleaving polygalacturonate, a major component of the pl ant 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 st rands coiled into a large helix. Within the core, the amino acids form linear stacks and include a novel asparagine ladder. The sequence sim ilarities that pectate lyases share with pectin lyases, pollen and sty le proteins, and tubulins suggest that the parallel beta helix motif m ay occur in a broad spectrum of proteins.