Document Detail

Modelling the three-dimensional structure and electrostatic potential field of the two Cu,Zn superoxide dismutase variants from Xenopus laevis.
MedLine Citation:
PMID:  1896428     Owner:  NLM     Status:  MEDLINE    
The crystallographic structure of bovine superoxide dismutase has been used as a template for the graphic reconstruction of the three-dimensional structures of the two Xenopus laevis variants (Schininà, M.E. et al. Arch. Biochem. Biophys. 272:507-515, 1989). In these models the structure-essential residues maintain their position and their structural role, and the interactions between the subunits and the close packing within the beta-barrel are maintained with conservative substitutions and even increased with "aromatic pairs." Because of the same topological motif and surface location of charges, arising from the model building of the two variants with respect to the bovine enzyme, we have calculated the electrostatic potential fields around the models of the two Xenopus laevis variants by numerically solving the Poisson-Boltzmann equation. We show that conservation of a specific space-relationship of charges maintains the potential field pattern already observed in the bovine enzyme, where a negative potential field surrounds the protein surface and specific positive regions wrap up the copper center active site. This electrostatic potential field distribution supports the idea that electrostatic interactions control, like in the bovine enzyme, the mechanism of enzyme-substrate recognition in the Xenopus laevis Cu,Zn superoxide dismutases, suggesting that coordinated mutation of charged residues has occurred in the evolution of this enzyme.
M Falconi; G Rotilio; A Desideri
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Proteins     Volume:  10     ISSN:  0887-3585     ISO Abbreviation:  Proteins     Publication Date:  1991  
Date Detail:
Created Date:  1991-10-23     Completed Date:  1991-10-23     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  8700181     Medline TA:  Proteins     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  149-55     Citation Subset:  IM    
Department of Biology, University of Rome Tor Vergata, Italy.
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MeSH Terms
Amino Acid Sequence
Binding Sites
Genetic Variation
Models, Molecular*
Molecular Sequence Data
Protein Conformation
Structure-Activity Relationship
Superoxide Dismutase / blood,  chemistry*
X-Ray Diffraction
Xenopus laevis
Reg. No./Substance:
EC Dismutase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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