1ibh
From Proteopedia
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X-RAY 3D STRUCTURE OF P.LEIOGNATHI CU,ZN SOD MUTANT M41I
Overview
The functional properties and X-ray structures of five mutant forms of, Photobacterium leiognathi Cu,Zn superoxide dismutase carrying single, mutations at residues located at the dimer association interface have been, investigated. When compared to the wild-type enzyme, the three-dimensional, structures of the mutants show structural perturbations limited to the, proximity of the mutation sites and substantial identity of active site, geometry. Nonetheless, the catalytic rates of all mutants, measured at, neutral pH and low ionic strength by pulse radiolysis, are higher than, that of the wild-type protein. Such enzymatic activity increase is, paralleled by enhanced active site accessibility to external chelating, agents, which, in the mutated enzyme, remove more readily the active site, copper ion. It is concluded that mutations at the prokaryotic Cu,Zn, superoxide dismutase subunit interface can transduce dynamical, perturbation to the active site region, promoting substrate active site, accessibility. Such long-range intramolecular communication effects have, not been extensively described before within the Cu,Zn superoxide, dismutase homology family.
About this Structure
1IBH 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 Full crystallographic information is available from OCA.
Reference
Single mutations at the subunit interface modulate copper reactivity in Photobacterium leiognathi Cu,Zn superoxide dismutase., Stroppolo ME, Pesce A, D'Orazio M, O'Neill P, Bordo D, Rosano C, Milani M, Battistoni A, Bolognesi M, Desideri A, J Mol Biol. 2001 May 4;308(3):555-63. PMID:11327787
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