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New Domain Motif: the Structure of Pectate Lyase C, a Secreted Plant Virulence Factor

Yoder, Marilyn D., Keen, Noel T., Jurnak, Frances·1993·Science

Abstract

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 β 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 β helix motif may occur in a broad spectrum of proteins.

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Metadata

Authors
Yoder, M. D., Keen, N. T., & Jurnak, F.
Venue
Science
Published
1993-06-04
Volume
260
Issue
5113
Pages
1503-1507
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2045476844
Cited by
453
References
0
FWCI
33.86
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: New Domain Motif: the Structure of Pectate Lyase C, a Secreted Plant Virulence Factor. https://app.cochat.ai/papers/10.1126/science.8502994
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Yoder, M. D., Keen, N. T., & Jurnak, F. (1993). New Domain Motif: the Structure of Pectate Lyase C, a Secreted Plant Virulence Factor. Science. https://doi.org/10.1126/science.8502994

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.