Abstract
The interaction between the type-II dockerin domain of the scaffoldin protein CipA and the type-II cohesin domain of the outer layer protein SdbA is the fundamental mechanism for anchoring the cellulosome to the cell surface of Clostridium thermocellum. We constructed and purified a dockerin polypeptide and a cohesin polypeptide, and determined affinity constants of the interaction between them by the surface plasmon resonance method. The dissociation constant (K(D)) value was 1.8 x 10(-9) M, which is a little larger than that for the combination of a type-I dockerin and a type-I cohesin.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Outer Membrane Proteins / chemistry
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Bacterial Outer Membrane Proteins / metabolism
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Bacterial Proteins / chemistry*
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Bacterial Proteins / metabolism*
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Cell Cycle Proteins
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Cellulosomes / chemistry*
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Cellulosomes / metabolism*
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Chromosomal Proteins, Non-Histone
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Clostridium / chemistry*
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Clostridium / metabolism
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Cohesins
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Fungal Proteins
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Membrane Proteins / chemistry
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Membrane Proteins / metabolism
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Nuclear Proteins / chemistry*
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Protein Binding
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Protein Structure, Tertiary
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Surface Plasmon Resonance
Substances
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Bacterial Outer Membrane Proteins
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Bacterial Proteins
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Cell Cycle Proteins
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Chromosomal Proteins, Non-Histone
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CipA protein, Clostridium
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Fungal Proteins
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Membrane Proteins
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Nuclear Proteins
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OlpB protein, Clostridium thermocellum
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SdbA protein, bacteria