On the structure of mitochondrial porins and its homologies with bacterial porins

Biochem Biophys Res Commun. 1994 Apr 29;200(2):908-15. doi: 10.1006/bbrc.1994.1536.

Abstract

By use of computer modelling, we have predicted a model of 16 transmembrane beta-strands for mitochondrial porins structure from human, Saccharomyces cerevisiae, Neurospora crassa and Dictyostelium discoideum. The proposed model takes into account biochemical and immunological data reported in the literature, as well as electrophysiological results obtained with yeast mitochondrial porins with mutations at selected amino acids. The predicted structure is very similar to that of some bacterial porins, as apparent from the homology of their hydropathic profiles.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Computer Simulation
  • Dictyostelium / chemistry
  • Dictyostelium / genetics
  • Escherichia coli / chemistry
  • Escherichia coli / genetics
  • Fungal Proteins / chemistry
  • Fungal Proteins / genetics
  • Humans
  • Membrane Proteins / chemistry*
  • Membrane Proteins / genetics*
  • Models, Chemical
  • Molecular Sequence Data
  • Molecular Structure
  • Neurospora crassa / chemistry
  • Neurospora crassa / genetics
  • Porins / chemistry*
  • Porins / genetics*
  • Protein Structure, Secondary
  • Protozoan Proteins / chemistry
  • Protozoan Proteins / genetics
  • Rhodobacter / chemistry
  • Rhodobacter / genetics
  • Saccharomyces cerevisiae / chemistry
  • Saccharomyces cerevisiae / genetics
  • Voltage-Dependent Anion Channels

Substances

  • Fungal Proteins
  • Membrane Proteins
  • Porins
  • Protozoan Proteins
  • Voltage-Dependent Anion Channels