Crystallization and preliminary X-ray diffraction analysis ofHypocrea jecorinaCel7A in two new crystal forms

Author:

Bodenheimer Annette M.,Cuneo Matthew J.,Swartz Paul D.,He Junhong,O'Neill Hugh M.,Myles Dean A. A.,Evans Barbara R.,Meilleur Flora

Abstract

Cel7A (previously known as cellobiohydrolase I) fromHypocrea jecorinawas crystallized in two crystalline forms, neither of which have been previously reported. Both forms co-crystallize under the same crystallization conditions. The first crystal form belonged to space groupC2, with unit-cell parametersa= 152.5,b= 44.9,c= 57.6 Å, β = 101.2°, and diffracted X-rays to 1.5 Å resolution. The second crystal form belonged to space groupP6322, with unit-cell parametersa=b≃ 155,c≃ 138 Å, and diffracted X-rays to 2.5 Å resolution. The crystals were obtained using full-length Cel7A, which consists of a large 434-residue N-terminal catalytic domain capable of cleaving cellulose, a 27-residue flexible linker and a small 36-residue C-terminal carbohydrate-binding module (CBM). However, a preliminary analysis of the electron-density maps suggests that the linker and CBM are disordered in both crystal forms. Complete refinement and structure analysis are currently in progress.

Publisher

International Union of Crystallography (IUCr)

Subject

Condensed Matter Physics,Genetics,Biochemistry,Structural Biology,Biophysics

Cited by 2 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

1. Crystal structures of wild‐type Trichoderma reesei Cel7A catalytic domain in open and closed states;FEBS Letters;2016-11-07

2. Glycosylation of Cellulases;Advances in Carbohydrate Chemistry and Biochemistry;2015

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