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Titolo:
CONFORMATIONAL-CHANGES IN THE MITOCHONDRIAL CHANNEL PROTEIN, VDAC, AND THEIR FUNCTIONAL IMPLICATIONS
Autore:
MANNELLA CA;
Indirizzi:
NEW YORK STATE DEPT HLTH,WADSWORTH CTR LABS & RES ALBANY NY 12201 SUNY ALBANY,SCH PUBL HLTH,DEPT BIOMED SCI ALBANY NY 12203
Titolo Testata:
Journal of structural biology
fascicolo: 2, volume: 121, anno: 1998,
pagine: 207 - 218
SICI:
1047-8477(1998)121:2<207:CITMCP>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
OUTER-MEMBRANE CHANNEL; ANION-SELECTIVE CHANNEL; RAT-LIVER MITOCHONDRIA; INTRAMITOCHONDRIALLY GENERATED ATP; NEUROSPORA-CRASSA MITOCHONDRIA; PEPTIDE-SPECIFIC ANTIBODIES; HEXOKINASE-BINDING PROTEIN; ESCHERICHIA-COLI; CRYSTALLINE ARRAYS; ELECTRON-MICROSCOPY;
Keywords:
CIRCULAR DICHROISM; CYTOCHROME C; ELECTRON MICROSCOPY; IMAGE PROCESSING; MITOCHONDRIA; PORIN; SEQUENCE ANALYSIS; 2-DIMENSIONAL CRYSTALS; VDAC; VOLTAGE-GATED ION CHANNEL;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
82
Recensione:
Indirizzi per estratti:
Citazione:
C.A. Mannella, "CONFORMATIONAL-CHANGES IN THE MITOCHONDRIAL CHANNEL PROTEIN, VDAC, AND THEIR FUNCTIONAL IMPLICATIONS", Journal of structural biology, 121(2), 1998, pp. 207-218

Abstract

The voltage-dependent, anion-selective channel (VDAC) is generally considered the main pathway for metabolite diffusion across the mitochondrial outer membrane. It also interacts with several mitochondrial andcytosolic proteins, including kinases and cytochrome c. Sequence analysis and circular dichroism suggest that the channel is a bacterial porin-like beta-barrel, However, unlike bacterial porins, VDAC does not form tight trimeric complexes and is easily gated (reversibly closed) by membrane potential and low pH. Circular dichroism indicates that the protein undergoes a major conformational change at pH <5, involving decreased beta-sheet and increased cw-helical content. Electron microscopy of two-dimensional crystals of fungal VDAC provides direct information about the size and shape of its lumen and suggests that the N-terminal domain forms a mobile alpha-helix, It is proposed that the N-terminal domain normally resides in a groove in the lumen wall and that gating stimuli favor its displacement, destabilizing the putative beta-barrel. Partial closure would result from subsequent larger-scale structural rearrangements in the protein, possibly corresponding to the conformational change observed at pH <5. (C) 1998 Academic Press.

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Documento generato il 30/03/20 alle ore 20:08:38