Evidence for a dual binding mode of dockerin modules to cohesins

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Evidence for a dual binding mode of dockerin modules to cohesins.

The assembly of proteins that display complementary activities into macromolecular complexes is critical to cellular function. One such enzyme complex, of environmental significance, is the plant cell wall degrading apparatus of anaerobic bacteria, termed the cellulosome. The complex assembles through the interaction of enzyme-derived "type I dockerin" modules with the multiple "cohesin" module...

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The Clostridium cellulolyticum dockerin displays a dual binding mode for its cohesin partner.

The plant cell wall degrading apparatus of anaerobic bacteria includes a large multienzyme complex termed the "cellulosome." The complex assembles through the interaction of enzyme-derived dockerin modules with the multiple cohesin modules of the noncatalytic scaffolding protein. Here we report the crystal structure of the Clostridium cellulolyticum cohesin-dockerin complex in two distinct orie...

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Resolving dual binding conformations of cellulosome cohesin-dockerin complexes using single-molecule force spectroscopy

Receptor-ligand pairs are ordinarily thought to interact through a lock and key mechanism, where a unique molecular conformation is formed upon binding. Contrary to this paradigm, cellulosomal cohesin-dockerin (Coh-Doc) pairs are believed to interact through redundant dual binding modes consisting of two distinct conformations. Here, we combined site-directed mutagenesis and single-molecule for...

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T-dual Rickart modules

We introduce the notions of T-dual Rickart and strongly T-dual Rickart modules. We provide several characterizations and investigate properties of each of these concepts. It is shown that every free (resp. finitely generated free) $R$-module is T-dual Rickart if and only if $overline{Z}^2(R)$ is a  direct summand of $R$ and End$(overline{Z}^2(R))$ is a semisimple (resp. regular) ring. It is sho...

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ژورنال

عنوان ژورنال: Proceedings of the National Academy of Sciences

سال: 2007

ISSN: 0027-8424,1091-6490

DOI: 10.1073/pnas.0611173104