EVOLUTIONARY CONSTRAINTS FOR DIMER FORMATION IN PROKARYOTIC CU, ZN SUPEROXIDE DISMUTASE
作者： Domenico Bordo , Dijana Matak , Kristina Djinovic-Carugo , Camillo Rosano , Alessandra Pesce
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摘要: Prokaryotic Cu,Zn superoxide dismutases are characterized by a distinct quaternary structure, as compared to that of the homologous eukaryotic enzymes. Here we report newly determined crystal structure dimeric dismutase from Photobacterium leiognathi (crystallized in space group R32, refined at 2.5 A resolution, R-factor 0.19) and analyse it comparison with monomeric enzyme Escherichia coli. The assembly, observed also previously studied monoclinic form P. dismutase, is based on ring-shaped subunit contact region, defining solvated interface cavity. Three clusters neighbouring residues play direct role stabilization assembly. present analysis, extended amino acid sequences other 11 known prokaryotic dismutases, shows least five enzymes residue under strong evolutionary constraint, suggesting attainment coincident dismutase. Calculation electrostatic fields for both E. coli monomeric/dimeric association behaviour displayed Cu, Zn related distribution surface charged residues. Moreover, Brownian dynamics simulations reproduce closely enzyme:substrate rates, highlighting active site determining catalytic properties.
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