1oaj

From Proteopedia

Revision as of 13:43, 30 October 2007

ACTIVE SITE COPPER AND ZINC IONS MODULATE THE QUATERNARY STRUCTURE OF PROKARYOTIC CU,ZN SUPEROXIDE DISMUTASE

Overview

The influence of the constitutive metal ions on the equilibrium properties, of dimeric Photobacterium leiognathi Cu,Zn superoxide dismutase has been, studied for the wild-type and for two mutant protein forms bearing a, negative charge in the amino acid clusters at the dimer association, interface. Depletion of copper and zinc dissociates the two mutant, proteins into monomers, which reassemble toward the dimeric state upon, addition of stoichiometric amounts of zinc. Pressure-dependent, dissociation is observed for the copper-depleted wild-type and mutated, enzymes, as monitored by the fluorescence shift of a unique tryptophan, residue located at the subunit association interface. The spectral shift, occurs slowly, reaching a plateau after 15-20 minutes, and is fully, reversible. The ... [(full description)]

About this Structure

1OAJ is a [Single protein] structure of sequence from [Photobacterium leiognathi] with ZN and CU as [ligands]. Active as [Superoxide dismutase], with EC number [1.15.1.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Active-site copper and zinc ions modulate the quaternary structure of prokaryotic Cu,Zn superoxide dismutase., Cioni P, Pesce A, Morozzo della Rocca B, Castelli S, Falconi M, Parrilli L, Bolognesi M, Strambini G, Desideri A, J Mol Biol. 2003 Mar 7;326(5):1351-60. PMID:12595249

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