Global Twisting Motion of Single Molecular KcsA Potassium Channel upon Gating.

Material type: 文書・図像類

Author: SHIMIZU, Hirofumiほか

Publisher: Elsevier

Publication date: 2008-01

Material Format: Digital

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Note (General)：: Ion channels are signal transduction molecules that switch ion permeation pathways on and off (gating). Crystal structures of several kinds of potassi...

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Material Type: 文書・図像類
Title: Global Twisting Motion of Single Molecular KcsA Potassium Channel upon Gating.
Author/Editor: SHIMIZU, Hirofumi
IWAMOTO, Masayuki
KONNO, Takashi
NIHEI, Amiko
SASAKI, Yuji C.
OIKI, Shigetoshi
Author Heading: SHIMIZU, Hirofumi
IWAMOTO, Masayuki
KONNO, Takashi
NIHEI, Amiko
SASAKI, Yuji C.
OIKI, Shigetoshi
Publication, Distribution, etc.: Elsevier
Publication Date: 2008-01
Publication Date (W3CDTF): 2008-01
Periodical title: Cell
No. or year of volume/issue: 132 1
Volume: 132
Issue: 1
Pages: 67-78
Text Language Code: eng
Subject Heading: PROTEINS
Target Audience: 一般
Note (General): Ion channels are signal transduction molecules that switch ion permeation pathways on and off (gating). Crystal structures of several kinds of potassium channels have revealed open and closed conformations, which provide static pictures of gating status. Here we studied KcsA potassium channels undergoing conformational changes at the single-molecule level. A KcsA channel with a gold nanocrystal attached was irradiated by white X-rays and motions of the diffraction spot from the nanocrystal were tracked in real time. Upon gating, the KcsA channels twisted around the axis of the pore. These conformational changes were prevented by an open-channel blocker, tetrabuthylammonium. Random clockwise and counterclockwise twisting in the range of several tens of degrees originated in the transmembrane domain and was transmitted to the cytoplasmic domain. This coupling suggests a mechanical interplay between the transmembrane and cytoplasmic domains.
Source: https://u-fukui.repo.nii.ac.jp/?action=repository_action_common_download&item_id=20579&item_no=1&attribute_id=22&file_no=1
https://u-fukui.repo.nii.ac.jp/?action=repository_action_common_download&item_id=20579&item_no=1&attribute_id=22&file_no=1
Access Restrictions: 限定公開
Related Material (DOI): 10.1016/j.cell.2007.11.040
Data Provider (Database): 国立情報学研究所 : 学術機関リポジトリデータベース（IRDB）（機関リポジトリ）
https://irdb.nii.ac.jp
Original Data Provider (Database): 福井大学 : 福井大学学術機関リポジトリ