Literature DB >> 2195018

Preliminary crystallographic analysis of the plant pathogenic factor, pectate lyase C from Erwinia chrysanthemi.

M D Yoder1, D A DeChaine, F Jurnak.   

Abstract

Pectate lyases are saccharide-binding enzymes that degrade plant cell walls. One pectate lyase from Erwinia chrysanthemi (EC16), termed pectate lyase C, has been crystallized from ammonium sulfate. The preliminary x-ray diffraction analysis indicates that the crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit cell dimensions, a = 73.4 A, b = 80.3 A, and c = 95.1 A. The crystals diffract to a resolution of 2.2 A and have one molecule/asymmetric unit.

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Year:  1990        PMID: 2195018

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  3 in total

1.  Structure of a plant cell wall fragment complexed to pectate lyase C.

Authors:  R D Scavetta; S R Herron; A T Hotchkiss; N Kita; N T Keen; J A Benen; H C Kester; J Visser; F Jurnak
Journal:  Plant Cell       Date:  1999-06       Impact factor: 11.277

2.  The Refined Three-Dimensional Structure of Pectate Lyase C from Erwinia chrysanthemi at 2.2 Angstrom Resolution (Implications for an Enzymatic Mechanism).

Authors:  M. D. Yoder; F. Jurnak
Journal:  Plant Physiol       Date:  1995-02       Impact factor: 8.340

3.  Combined transcriptomic and proteomic analysis reveals multiple pathways involved in self-pollen tube development and the potential roles of FviYABBY1 in self-incompatibility in Fragaria viridis.

Authors:  Jianke Du; Chunfeng Ge; Tao Wang; Jing Wang; Zhiyou Ni; Shiwei Xiao; Fengli Zhao; Mizhen Zhao; Yushan Qiao
Journal:  Front Plant Sci       Date:  2022-09-14       Impact factor: 6.627

  3 in total

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