Effect of carboxylate-binding mode on metal binding/selectivity and function in proteins.

Todor Dudev, Carmay Lim
Author Information
  1. Todor Dudev: Institute of Biomedical Sciences, Academia Sinica, Taipei 115, Taiwan.

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.

MeSH Term

Carboxylic Acids
Cations
Models, Molecular
Protein Binding
Proteins
Thermodynamics

Chemicals

Carboxylic Acids
Cations
Proteins

Word Cloud

Similar Articles

Cited By