The interaction of Glu294 at the subunit interface is important for the activity and stability of goose delta-crystallin.

ABSTRACT:

Purpose

delta-Crystallin is a soluble structural protein in found in avian eye lenses; it shares high amino acid sequence identity with argininosuccinate lyase. E294 is the only residue located at the double dimer interface and it performs hydrogen bonding with the active site residues of H160 and K323 in the neighboring and diagonal subunits, respectively. H160 is reported to play an important role in catalysis due to its H-bond interaction with the fumarate moiety of the substrate. In order to clarify the function of E294 in either stabilization of the quaternary structure or in catalysis, we carried out site-directed mutagenesis and functional analysis.

Methods

The structure of both wild-type and mutant proteins were analyzed by circular dichroism (CD) spectroscopy, fluor

SUBMITTER: Huang CW 

PROVIDER: S-EPMC2779060 | biostudies-literature | 2009 Nov

REPOSITORIES: biostudies-literature