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The role of solution NMR in the structure determinations of VDAC-1 and other membrane proteins

Hiller, Sebastian and Wagner, Gerhard. (2009) The role of solution NMR in the structure determinations of VDAC-1 and other membrane proteins. Current opinion in structural biology, 19 (4). pp. 396-401.

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Official URL: http://edoc.unibas.ch/41074/

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Abstract

The voltage-dependent anion channel (VDAC) is an essential protein in the eukaryotic outer mitochondrial membrane, providing the pore for substrate diffusion. Three high-resolution structures of the isoform 1 of VDAC in detergent micelles and bicelles have recently been published, using solution NMR and X-ray crystallography. They resolve longstanding discussions about the membrane topology of VDAC and provide the first eukaryotic beta-barrel membrane protein structure. The structure contains a surprising feature that had not been observed in an integral membrane protein before: A parallel beta-strand pairing and thus an odd number of strands. The studies also give a structural and functional basis for the voltage gating mechanism of VDAC and its modulation by NADH; however, they do not fully explain these functions yet. With the de novo structure of VDAC-1, as well as those of half a dozen other proteins, the number of integral membrane protein structures solved by solution NMR has doubled in the past two years. Numerous further structural and functional studies on many different membrane proteins show that solution NMR has become an important tool for membrane protein molecular biology.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Hiller)
UniBasel Contributors:Hiller Odermatt, Sebastian
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Current Biology
ISSN:0959-440X
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:19 Dec 2017 13:43
Deposited On:17 Aug 2016 09:13

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