Abstract
A very short hydrogen bond between an Asp and a phosphate is established in two high resolution structures (0.98 and 1.05 A). A mutant complex that changes the Asp to an Asn, which forms a normal hydrogen bond, has a similar free energy of binding to the wild type complex, suggesting that the contribution of the short hydrogen bond is not extraordinarily strong.
Publication types
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Letter
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Carrier Proteins / chemistry*
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Carrier Proteins / genetics
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Carrier Proteins / metabolism*
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Crystallography, X-Ray
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Hydrogen Bonding
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Hydrogen-Ion Concentration
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Models, Molecular
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Mutation
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Phosphate-Binding Proteins
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Phosphates / chemistry*
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Phosphates / metabolism*
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Protein Conformation
Substances
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Carrier Proteins
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Phosphate-Binding Proteins
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Phosphates