Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form
As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website. Faculty profile pages will continue to be updated via Interfolio. VIVO will continue being used behind the scenes to update graduate student profiles. Please contact helplib@scripps.edu if you have questions.
How to download citations from VIVO | Alternative profile options

Evolution of Cu Zn superoxide-dismutase and the Greek key beta-barrel structural motif

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Getzoff, Elizabeth
  • Tainer, John
  • Stempien, M. M.
  • Bell, G. I.
  • Hallewell, R. A.

publication date

  • 1989

journal

  • Proteins-Structure Function and Genetics  Journal

abstract

  • Detailed analysis of the CuZn superoxide dismutase (SOD) structure provides new results concerning the significance and molecular basis for sequence conservation, intron-exon boundary locations, gene duplication, and Greek key beta-barrel evolution. Using 15 aligned sequences, including a new mouse sequence, specific roles have been assigned to all 23 invariant residues and additional residues exhibiting functional equivalence. Sequence invariance is dominated by 15 residues that form the active site stereochemistry, supporting a primary biological function of superoxide dismutation. The beta-strands have no sequence insertions and deletions, whereas insertions occur within the loops connecting the beta-strands and at both termini. Thus, the beta-barrel with only four invariant residues is apparently over-determined, but dependent on multiple cooperative side chain interactions. The regions encoded by exon I, a proposed nucleation site for protein folding, and exon III, the Zn loop involved in stability and catalysis, are the major structural subdomains not included in the internal twofold axis of symmetry passing near the catalytic Cu ion. This provides strong confirmatory evidence for gene evolution by duplication and fusion followed by the addition of these two exons. The proposed evolutionary pathway explains the structural versatility of the Greek key beta-barrel through functional specialization and subdomain insertions in new loop connections, and provides a rationale for the size of the present day enzyme.

subject areas

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Biological Evolution
  • Computer Graphics
  • DNA
  • Female
  • Genetic Variation
  • Humans
  • Mice
  • Models, Molecular
  • Molecular Sequence Data
  • Placenta
  • Pregnancy
  • Protein Conformation
  • Recombinant Proteins
  • Sequence Homology, Nucleic Acid
  • Superoxide Dismutase
  • X-Ray Diffraction
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0887-3585

Digital Object Identifier (DOI)

  • 10.1002/prot.340050408

PubMed ID

  • 2798409
scroll to property group menus

Additional Document Info

start page

  • 322

end page

  • 336

volume

  • 5

issue

  • 4

©2022 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support