Cohesin-dockerin recognition in cellulosome assembly: experiment versus hypothesis.
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 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.
Mechaly
A
A
Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot, Israel.
Yaron
S
S
Lamed
R
R
Fierobe
H P
HP
Belaich
A
A
Belaich
J P
JP
Shoham
Y
Y
Bayer
E A
EA
D000345:Affinity Labels; D019943:Amino Acid Substitution; D001407:Bacillus / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D002480:Cellulase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D003013:Clostridium / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D015335:Molecular Probes / Q000737:chemistry / Q000378:metabolism; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D011485:Protein Binding; D017434:Protein Structure, Tertiary / Q000235:genetics; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity
D000345:Affinity Labels; D001426:Bacterial Proteins; C080369:CipA protein, Clostridium; D008565:Membrane Proteins; D015335:Molecular Probes; C071223:endoglucanase Ss; C074775:CelA endoglucanase; D002480:Cellulase