Effect of carboxylate-binding mode on metal binding/selectivity and function in proteins |
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Authors: | Dudev Todor Lim Carmay |
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Affiliation: | Institute of Biomedical Sciences, Academia Sinica, Taipei 115, Taiwan. |
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Abstract: | We delineate the factors governing the carboxylate-binding mode (monodentate vs bidentate) in metalloproteins. We reveal how the carboxylate-binding mode affects the binding affinity and selectivity of a metal ion as well as the function of a metalloprotein using Ca2+-binding proteins and enzymes (ribonuclease H1, phosphoserine phosphatase, and ribonucleotide reductase) as examples. The collected data indicate that a carboxylate monodentate left arrow over right arrow bidentate switch, in addition to other structural factors, could be used to fine tune the metal-binding site affinity and/or selectivity, thus modifying the function/properties of the metalloprotein. |
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