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Proteins. 2000 May 1;39(2):170-7.

Cohesin-dockerin recognition in cellulosome assembly: experiment versus hypothesis.

Author information

1
Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot, Israel.

Abstract

The cohesin-dockerin interaction provides the basis for incorporation of the individual enzymatic subunits into the cellulosome complex. In a previous article (Pag├ęs et al., Proteins 1997;29:517-527) we predicted that four amino acid residues of the approximately 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.

PMID:
10737938
[Indexed for MEDLINE]

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