Hinge-bending in L-arabinose-binding protein. The "Venus's-flytrap" model.

B Mao; M R Pear; J A McCammon; F A Quiocho

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PubMed · 7035444

Hinge-bending in L-arabinose-binding protein. The "Venus's-flytrap" model.

B Mao·M R Pear·J A McCammon·F A Quiocho

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Abstract

Theoretical conformational energy calculations show that large changes in the width of the binding-site cleft in the L-arabinose-binding protein involve only modest changes in the protein internal energy. Solvation energy changes associated with such variations of the cleft width and with protein-ligand interactions are estimated to be significantly larger than the internal energy changes. These results indicate that the binding-site cleft is open in the unliganded protein and is induced to close upon ligation. This picture is consistent with experimental data on the structure and binding kinetics of the L-arabinose-binding protein and provides a physical framework for interpreting such data.

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Bacterial Proteins Binding Sites Carrier Proteins Escherichia coli Escherichia coli Proteins Models, Molecular Protein Conformation Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.Research Support, U.S. Gov't, P.H.S.

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B Mao, M R Pear, J A McCammon, F A Quiocho. 1982-02-10. Hinge-bending in L-arabinose-binding protein. The "Venus's-flytrap" model.. https://pubmed.ncbi.nlm.nih.gov/7035444/

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