Abstract
Carbohydrate-binding modules (CBMs) are key components of many carbohydrate-modifying enzymes. CBMs affect the activity of these enzymes by modulating bonding and catalysis. To further characterize and study CBM-ligand binding interactions, neutron crystallographic studies of an engineered family 4-type CBM in complex with a branched xyloglucan ligand were conducted. The first neutron crystal structure of a CBM-ligand complex reported here shows numerous atomic details of hydrogen bonding and water-mediated interactions and reveals the charged state of key binding cleft amino acid side chains.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / chemistry
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Bacterial Proteins / metabolism
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Binding Sites
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Carbohydrate Metabolism*
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Carbohydrates / chemistry*
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Catalytic Domain
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Crystallography, X-Ray
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Endo-1,4-beta Xylanases / chemistry*
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Endo-1,4-beta Xylanases / metabolism*
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Enzymes / chemistry
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Enzymes / metabolism
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Glucans / chemistry
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Glucans / metabolism
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Hydrogen Bonding
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Ligands
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Models, Molecular
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Neutrons
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Protein Binding
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Receptors, Cell Surface / chemistry
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Receptors, Cell Surface / metabolism
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Rhodothermus / enzymology
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Water
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Xylans / chemistry
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Xylans / metabolism
Substances
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Bacterial Proteins
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Carbohydrates
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Enzymes
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Glucans
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Ligands
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Receptors, Cell Surface
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Xylans
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saccharide-binding proteins
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Water
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xyloglucan
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Endo-1,4-beta Xylanases