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来自菊欧文氏菌的植物致病因子果胶酸裂解酶C的初步晶体学分析。

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

作者信息

Yoder M D, DeChaine D A, Jurnak F

机构信息

Department of Biochemistry, University of California, Riverside 92521.

出版信息

J Biol Chem. 1990 Jul 15;265(20):11429-31.

PMID:2195018
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.

摘要

果胶酸裂解酶是一类能降解植物细胞壁的糖类结合酶。一种来自菊欧文氏菌(EC16)的果胶酸裂解酶,称为果胶酸裂解酶C,已通过硫酸铵结晶。初步的X射线衍射分析表明,这些晶体属于正交晶系空间群P2(1)2(1)2(1),晶胞参数为a = 73.4 Å,b = 80.3 Å,c = 95.1 Å。这些晶体的衍射分辨率为2.2 Å,每个不对称单位含有一个分子。

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J Biol Chem. 1990 Jul 15;265(20):11429-31.
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Preliminary crystallographic analysis of a plant pathogenic factor: pectate lyase.
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Structure of two pectate lyase genes from Erwinia chrysanthemi EC16 and their high-level expression in Escherichia coli.来自菊欧文氏菌EC16的两个果胶酸裂解酶基因的结构及其在大肠杆菌中的高效表达。
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The Refined Three-Dimensional Structure of Pectate Lyase C from Erwinia chrysanthemi at 2.2 Angstrom Resolution (Implications for an Enzymatic Mechanism).来自菊欧文氏菌的果胶酸裂合酶C在2.2埃分辨率下的精细三维结构(对酶作用机制的启示)
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Structure of a plant cell wall fragment complexed to pectate lyase C.
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Plant Cell. 1999 Jun;11(6):1081-92. doi: 10.1105/tpc.11.6.1081.