Literature DB >> 9761829

Crystallization of the catalytic domain of Clostridium cellulolyticum CeLF cellulase in the presence of a newly synthesized cellulase inhibitor.

C Reverbel-Leroy1, G Parsiegla, V Moreau, M Juy, C Tardif, H Driguez, J P Bélaich, R Haser.   

Abstract

The catalytic domain of the CeIF processive endocellulase, a family 48 glycosyl hydrolase from Clostridium cellulolyticum has been crystallized in the presence of a newly synthesized inhibitor (methyl 4-S-beta-cellobiosyl-4-thio-beta-cellobioside), by vapour diffusion, using PEG as a precipitant. The protein crystallizes in the orthorhombic P212121 space group and diffracts to a resolution of 2.0 A. The unit-cell parameters are a = 61.4, b = 84.5, c = 121.9 A.

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Year:  1998        PMID： 9761829     DOI： 10.1107/s090744499700797x

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN： 0907-4449


  3 in total

1.  Structural basis for broad substrate specificity in higher plant beta-D-glucan glucohydrolases.

Authors:  Maria Hrmova; Ross De Gori; Brian J Smith; Jon K Fairweather; Hugues Driguez; Joseph N Varghese; Geoffrey B Fincher
Journal:  Plant Cell       Date:  2002-05       Impact factor: 11.277

2.  Two-parameter kinetic model based on a time-dependent activity coefficient accurately describes enzymatic cellulose digestion.

Authors:  Maxim Kostylev; David Wilson
Journal:  Biochemistry       Date:  2013-07-24       Impact factor: 3.162

3.  The crystal structure of the processive endocellulase CelF of Clostridium cellulolyticum in complex with a thiooligosaccharide inhibitor at 2.0 A resolution.

Authors:  G Parsiegla; M Juy; C Reverbel-Leroy; C Tardif; J P Belaïch; H Driguez; R Haser
Journal:  EMBO J       Date:  1998-10-01       Impact factor: 11.598
  3 in total

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