Effect of carboxylate-binding mode on metal binding/selectivity and function in proteins.
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.
Dudev
Todor
T
Institute of Biomedical Sciences, Academia Sinica, Taipei 115, Taiwan.
Lim
Carmay
C
D002264:Carboxylic Acids / Q000378:metabolism*; D002412:Cations; D008958:Models, Molecular; D011485:Protein Binding; D011506:Proteins / Q000502:physiology*; D013816:Thermodynamics
D002264:Carboxylic Acids; D002412:Cations; D011506:Proteins