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Cohesin-dockerin recognition in cellulosome assembly: Experiment versus hypothesis
- Source :
- Proteins: Structure, Function, and Genetics. 39:170-177
- Publication Year :
- 2000
- Publisher :
- Wiley, 2000.
-
Abstract
- The cohesin-dockerin interaction provides the basis for incorporation of the indi- vidual enzymatic subunits into the cellulosome com- plex. In a previous article (Pages 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 exam- ined by site-directed mutagenesis of the suspected residues, whereby the species-specificity of the cohe- sin-dockerin interaction was altered. The results support the premise that the four residues indeed play a role in biorecognition, while additional resi- dues may also contribute to the specificity of the interaction. Proteins 2000;39:170 -177.
Details
- ISSN :
- 10970134 and 08873585
- Volume :
- 39
- Database :
- OpenAIRE
- Journal :
- Proteins: Structure, Function, and Genetics
- Accession number :
- edsair.doi...........235f3b130338117ec4c00a2cb647bf67
- Full Text :
- https://doi.org/10.1002/(sici)1097-0134(20000501)39:2<170::aid-prot7>3.0.co;2-h