Metal-binding sites are designed to achieve optimal mechanical and signaling properties.

ABSTRACT: Many proteins require bound metals to achieve their function. We take advantage of increasing structural data on metal-binding proteins to elucidate three properties: the involvement of metal-binding sites in the global dynamics of the protein, predicted by elastic network models, their exposure/burial to solvent, and their signal-processing properties indicated by Markovian stochastics analysis. Systematic analysis of a data set of 145 structures reveals that the residues that coordinate metal ions enjoy remarkably efficient and precise signal transduction properties. These properties are rationalized in terms of their physical properties: participation in hinge sites that control the softest modes collectively accessible to the protein and occupancy of central positions minimally exposed

SUBMITTER: Dutta A 

PROVIDER: S-EPMC2937013 | biostudies-literature | 2010 Sep

REPOSITORIES: biostudies-literature