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Preliminary crystallographic analysis of a plant pathogenic factor: pectate lyase.

作者信息

Kim C Y, Mosser V, Keen N, Jurnak F

机构信息

Department of Biochemistry, University of California, Riverside 92521.

出版信息

J Mol Biol. 1989 Jul 20;208(2):365-7. doi: 10.1016/0022-2836(89)90397-5.

DOI:10.1016/0022-2836(89)90397-5
PMID:2769765
Abstract

Pectate lyase is a saccharide-binding enzyme that lyitically depolymerizes polypectate in higher plant cell walls, thus causing soft-rot diseases in food crops. A pectate lyase from Erwinia chrysanthemi, EC16 (PLe), crystallizes in the orthorhombic space group P2(1)2(1)2(1) with unit cell dimension of a = 39.0 A, b = 91.0 A and c = 103.4 A. The asymmetric unit consists of one molecule with a molecular mass of 38,118 daltons and the X-ray diffraction extends to a resolution of 1.8 A. The crystals reproducibly grow to large dimensions and are suitable for a high-resolution X-ray diffraction analysis.

摘要

相似文献

1
Preliminary crystallographic analysis of a plant pathogenic factor: pectate lyase.
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2
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J Mol Biol. 1992 Dec 20;228(4):1255-8. doi: 10.1016/0022-2836(92)90330-m.

引用本文的文献

1
The Three-Dimensional Structure of Pectate Lyase E, a Plant Virulence Factor from Erwinia chrysanthemi.来自菊欧文氏菌的植物致病因子果胶酸裂解酶E的三维结构
Plant Physiol. 1994 Nov;106(3):849-862. doi: 10.1104/pp.106.3.849.
2
The Refined Three-Dimensional Structure of Pectate Lyase E from Erwinia chrysanthemi at 2.2 A Resolution.来自菊欧文氏菌的果胶酸裂解酶E在2.2埃分辨率下的精细三维结构
Plant Physiol. 1996 May;111(1):73-92. doi: 10.1104/pp.111.1.73.