ArticleBiophysical journal2006
Deletion variants of Neurospora mitochondrial porin: electrophysiological and spectroscopic analysis.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 20 citations in OpenAlex.
- Gating of β-Barrel Protein Pores, Porins, and Channels: An Old Problem with New Facets.International journal of molecular sciences · 2023Review
- Historical Perspective of Pore-Forming Activity Studies of Voltage-Dependent Anion Channel (Eukaryotic or Mitochondrial Porin) Since Its Discovery in the 70th of the Last Century.Frontiers in physiology · 2021Review
- A Cholesterol Analog Induces an Oligomeric Reorganization of VDAC.Biophysical journal · 2019Article
- Solid-state NMR, electrophysiology and molecular dynamics characterization of human VDAC2.Journal of biomolecular NMR · 2015Article
- β-Barrel mobility underlies closure of the voltage-dependent anion channel.Structure (London, England : 1993) · 2012Article
- VDAC structure, selectivity, and dynamics.Biochimica et biophysica acta · 2012Review
- The 3D structures of VDAC represent a native conformation.Trends in biochemical sciences · 2010Review
- Two-step folding of recombinant mitochondrial porin in detergent.Biophysical journal · 2008Article
- The evolutionary history of mitochondrial porins.BMC evolutionary biology · 2007Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mitochondrial porins are predicted to traverse the outer membrane as a series of beta-strands, but the precise structure of the resulting beta-barrel has remained elusive. Toward determining the positions of the membrane-spanning segments, a series of small deletions was introduced into several of the predicted beta-strands of the Neurospora crassa porin. Overall, three classes of porin variants were identified: i), those producing large, stable pores, indicating deletions likely outside of beta-strands; ii), those with minimal pore-forming ability, indicating disruptions in key beta-strands or beta-turns; and iii), those that formed small unstable pores with a variety of gating and ion-selectivity properties. The latter class presumably results from a subset of proteins that adopt an alternative barrel structure upon the loss of stabilizing residues. Some variants were not sufficiently stable in detergent for structural analysis; circular dichroism spectropolarimetry of those that were did not reveal significant differences in the overall structural composition among the detergent-solubilized porin variants and the wild-type protein. Several of the variants displayed altered tryptophan fluorescence profiles, indicative of differing microenvironments surrounding these residues. Based on these results, modifications to the existing models for porin structure are proposed.
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