Use of anion-aromatic interactions to position the general base in the ketosteroid isomerase active site.

ABSTRACT: Although the cation-pi pair, formed between a side chain or substrate cation and the negative electrostatic potential of a pi system on the face of an aromatic ring, has been widely discussed and has been shown to be important in protein structure and protein-ligand interactions, there has been little discussion of the potential structural and functional importance in proteins of the related anion-aromatic pair (i.e., interaction of a negatively charged group with the positive electrostatic potential on the ring edge of an aromatic group). We posited, based on prior structural information, that anion-aromatic interactions between the anionic Asp general base and Phe54 and Phe116 might be used instead of a hydrogen-bond network to position the general base in the active site of ketosteroid

SUBMITTER: Schwans JP 

PROVIDER: S-EPMC3710852 | biostudies-literature | 2013 Jul

REPOSITORIES: biostudies-literature