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Research Article
Cohesin-dockerin recognition in cellulosome assembly: Experiment versus hypothesis
Article first published online: 24 MAR 2000
DOI: 10.1002/(SICI)1097-0134(20000501)39:2<170::AID-PROT7>3.0.CO;2-H
Copyright © 2000 Wiley-Liss, Inc.
Issue
1097-0134/asset/cover.gif?v=1&s=d817e79b67ba6cacf8bdcce1a819c04de300a7e3 "Proteins: Structure, Function, and Bioinformatics")
Proteins: Structure, Function, and Bioinformatics
Volume 39, Issue 2, pages 170–177, 1 May 2000
Additional Information
How to Cite
Mechaly, A., Yaron, S., Lamed, R., Fierobe, H.-P., Belaich, A., Belaich, J.-P., Shoham, Y. and Bayer, E. A. (2000), Cohesin-dockerin recognition in cellulosome assembly: Experiment versus hypothesis. Proteins, 39: 170–177. doi: 10.1002/(SICI)1097-0134(20000501)39:2<170::AID-PROT7>3.0.CO;2-H
Publication History
- Issue published online: 24 MAR 2000
- Article first published online: 24 MAR 2000
- Manuscript Accepted: 14 DEC 1999
- Manuscript Received: 12 OCT 1999
- Abstract
- Article
- References
- Cited By
Keywords:
- cellulosome;
- cellulases;
- multi-enzyme complex;
- scaffoldin subunit;
- protein-protein interaction;
- Clostridium thermocellum;
- Clostridium cellulolyticum
Abstract
The cohesin-dockerin interaction provides the basis for incorporation of the individual enzymatic subunits into the cellulosome complex. In a previous article (Pagés et al., Proteins 1997;29:517–527) we predicted that four amino acid residues of the ∼70-residue dockerin domain would serve as recognition codes for binding to the cohesin domain. The validity of the prediction was examined by site-directed mutagenesis of the suspected residues, whereby the species-specificity of the cohesin-dockerin interaction was altered. The results support the premise that the four residues indeed play a role in biorecognition, while additional residues may also contribute to the specificity of the interaction. Proteins 2000;39:170–177. © 2000 Wiley-Liss, Inc.