Affixing N-terminal a-helix to the wall of the voltage-dependent anion channel does not prevent its voltage gating

Teijido Hermida, Óscar; Ujwal, Rachna; Hillerdal, Carl-Olof; Kullman, Lisen; Rostovtseva, Tatiana K.; Abramson, Jeff

Affixing N-terminal a-helix to the wall of the voltage-dependent anion channel does not prevent its voltage gating

dc.contributor.author	Teijido Hermida, Óscar
dc.contributor.author	Ujwal, Rachna
dc.contributor.author	Hillerdal, Carl-Olof
dc.contributor.author	Kullman, Lisen
dc.contributor.author	Rostovtseva, Tatiana K.
dc.contributor.author	Abramson, Jeff
dc.contributor.department	Ciencias de la Salud	es_ES
dc.contributor.department	Osasun Zientziak	eu
dc.date.accessioned	2025-01-29T09:09:25Z
dc.date.available	2025-01-29T09:09:25Z
dc.date.issued	2012-03-30
dc.date.updated	2025-01-29T08:54:38Z
dc.description.abstract	The voltage-dependent anion channel (VDAC) governs the free exchange of ions and metabolites between the mitochondria and the rest of the cell. The three-dimensional structure of VDAC1 reveals a channel formed by 19 β-strands and an N-terminal α-helix located near the midpoint of the pore. The position of this α-helix causes a narrowing of the cavity, but ample space for metabolite passage remains. The participation of the N-terminus of VDAC1 in the voltage-gating process has been well established, but the molecular mechanism continues to be debated; however, the majority of models entail large conformational changes of this N-terminal segment. Here we report that the pore-lining N-terminal α-helix does not undergo independent structural rearrangements during channel gating. We engineered a double Cys mutant in murine VDAC1 that cross-links the α-helix to the wall of the β-barrel pore and reconstituted the modified protein into planar lipid bilayers. The modified murine VDAC1 exhibited typical voltage gating. These results suggest that the N-terminal α-helix is located inside the pore of VDAC in the open state and remains associated with β-strand 11 of the pore wall during voltage gating	en
dc.description.sponsorship	This work was supported, in whole or in part, by the Intramural Research Program of the Eunice Kennedy Shriver NICHD, National Institutes of Health (to O. T. and T. K. R.) and National Institutes of Health Grant RO1 GM078844 (to J. A.).
dc.format.mimetype	application/pdf	en
dc.format.mimetype	application/zip	en
dc.identifier.citation	Teijido, O., Ujwal, R., Hillerdal, C. O., Kullman, L., Rostovtseva, T. K., Abramson, J. (2012). Affixing N-terminal a-helix to the wall of the voltage-dependent anion channel does not prevent its voltage gating. Journal of the Biological Chemistry, 287(14), 11437-11445. https://doi.org/10.1074/jbc.M111.314229.
dc.identifier.doi	10.1074/jbc.M111.314229
dc.identifier.issn	0021-9258
dc.identifier.uri	https://academica-e.unavarra.es/handle/2454/53142
dc.language.iso	eng
dc.publisher	Elsevier
dc.relation.ispartof	Journal of the Biological Chemistry (2012), vol. 287, núm. 14
dc.relation.publisherversion	https://doi.org/10.1074/jbc.M111.314229
dc.rights	This is an open access article under the CC BY license.
dc.rights.accessRights	info:eu-repo/semantics/openAccess
dc.rights.uri	https://creativecommons.org/licenses/by/4.0/
dc.subject	ADP	en
dc.subject	ATP	en
dc.subject	Bioenergetics	en
dc.subject	Biophysics	en
dc.subject	Structural biology	en
dc.subject	Structural dynamics	en
dc.subject	Voltage dependency	en
dc.subject	Voltage-dependent anion channel	en
dc.title	Affixing N-terminal a-helix to the wall of the voltage-dependent anion channel does not prevent its voltage gating	en
dc.type	info:eu-repo/semantics/article
dc.type.version	info:eu-repo/semantics/publishedVersion
dspace.entity.type	Publication
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