English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Beta-barrel mobility underlies closure of the voltage-dependent anion channel.

Zachariae, U., Schneider, R., Briones, R., Gattin, Z., Demers, J. P., Giller, K., et al. (2012). Beta-barrel mobility underlies closure of the voltage-dependent anion channel. Structure, 20(9), 1540-1549. doi:10.1016/j.str.2012.06.015.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-000F-A67C-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-1F48-6
Genre: Journal Article

Files

show Files
hide Files
:
1481428.pdf (Publisher version), 4MB
Name:
1481428.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
1481428_Supplement.pdf (Supplementary material), 358KB
Name:
1481428_Supplement.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Creators

show
hide
 Creators:
Zachariae, U.1, Author              
Schneider, R.2, Author              
Briones, R.1, Author              
Gattin, Z.3, Author              
Demers, J. P.3, Author              
Giller, K.2, Author              
Maier, E., Author
Zweckstetter, M.4, Author              
Griesinger, C.2, Author              
Becker, S.2, Author              
Benz, R., Author
de Groot, B. L.1, Author              
Lange, A.3, Author              
Affiliations:
1Research Group of Computational Biomolecular Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578573              
2Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              
3Research Group of Solid-state NMR, MPI for biophysical chemistry, Max Planck Society, ou_persistent35              
4Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              

Content

show
hide
Free keywords: -
 Abstract: The voltage-dependent anion channel (VDAC) is the major protein in the outer mitochondrial membrane, where it mediates transport of ATP and ADP. Changes in its permeability, induced by voltage or apoptosis-related proteins, have been implicated in apoptotic pathways. The three-dimensional structure of VDAC has recently been determined as a 19-stranded β-barrel with an in-lying N-terminal helix. However, its gating mechanism is still unclear. Using solid-state NMR spectroscopy, molecular dynamics simulations, and electrophysiology, we show that deletion of the rigid N-terminal helix sharply increases overall motion in VDAC's β-barrel, resulting in elliptic, semicollapsed barrel shapes. These states quantitatively reproduce conductance and selectivity of the closed VDAC conformation. Mutation of the N-terminal helix leads to a phenotype intermediate to the open and closed states. These data suggest that the N-terminal helix controls entry into elliptic β-barrel states which underlie VDAC closure. Our results also indicate that β-barrel channels are intrinsically flexible.

Details

show
hide
Language(s): eng - English
 Dates: 2012-09-05
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.str.2012.06.015
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Structure
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 20 (9) Sequence Number: - Start / End Page: 1540 - 1549 Identifier: -