In:
PLOS Biology, Public Library of Science (PLoS), Vol. 19, No. 4 ( 2021-4-27), p. e3001231-
Abstract:
MgtE is a Mg 2+ channel conserved in organisms ranging from prokaryotes to eukaryotes, including humans, and plays an important role in Mg 2+ homeostasis. The previously determined MgtE structures in the Mg 2+ -bound, closed-state, and structure-based functional analyses of MgtE revealed that the binding of Mg 2+ ions to the MgtE cytoplasmic domain induces channel inactivation to maintain Mg 2+ homeostasis. There are no structures of the transmembrane (TM) domain for MgtE in Mg 2+ -free conditions, and the pore-opening mechanism has thus remained unclear. Here, we determined the cryo-electron microscopy (cryo-EM) structure of the MgtE-Fab complex in the absence of Mg 2+ ions. The Mg 2+ -free MgtE TM domain structure and its comparison with the Mg 2+ -bound, closed-state structure, together with functional analyses, showed the Mg 2+ -dependent pore opening of MgtE on the cytoplasmic side and revealed the kink motions of the TM2 and TM5 helices at the glycine residues, which are important for channel activity. Overall, our work provides structure-based mechanistic insights into the channel gating of MgtE.
Type of Medium:
Online Resource
ISSN:
1545-7885
DOI:
10.1371/journal.pbio.3001231
DOI:
10.1371/journal.pbio.3001231.g001
DOI:
10.1371/journal.pbio.3001231.g002
DOI:
10.1371/journal.pbio.3001231.g003
DOI:
10.1371/journal.pbio.3001231.g004
DOI:
10.1371/journal.pbio.3001231.g005
DOI:
10.1371/journal.pbio.3001231.g006
DOI:
10.1371/journal.pbio.3001231.g007
DOI:
10.1371/journal.pbio.3001231.s001
DOI:
10.1371/journal.pbio.3001231.s002
DOI:
10.1371/journal.pbio.3001231.s003
DOI:
10.1371/journal.pbio.3001231.s004
DOI:
10.1371/journal.pbio.3001231.s005
DOI:
10.1371/journal.pbio.3001231.s006
DOI:
10.1371/journal.pbio.3001231.s007
DOI:
10.1371/journal.pbio.3001231.s008
DOI:
10.1371/journal.pbio.3001231.s009
DOI:
10.1371/journal.pbio.3001231.s010
DOI:
10.1371/journal.pbio.3001231.s011
DOI:
10.1371/journal.pbio.3001231.s012
DOI:
10.1371/journal.pbio.3001231.s013
DOI:
10.1371/journal.pbio.3001231.s014
DOI:
10.1371/journal.pbio.3001231.s015
DOI:
10.1371/journal.pbio.3001231.s016
DOI:
10.1371/journal.pbio.3001231.s017
DOI:
10.1371/journal.pbio.3001231.s018
DOI:
10.1371/journal.pbio.3001231.s019
DOI:
10.1371/journal.pbio.3001231.s020
DOI:
10.1371/journal.pbio.3001231.s021
DOI:
10.1371/journal.pbio.3001231.s022
DOI:
10.1371/journal.pbio.3001231.s023
DOI:
10.1371/journal.pbio.3001231.r001
DOI:
10.1371/journal.pbio.3001231.r002
DOI:
10.1371/journal.pbio.3001231.r003
DOI:
10.1371/journal.pbio.3001231.r004
DOI:
10.1371/journal.pbio.3001231.r005
DOI:
10.1371/journal.pbio.3001231.r006
DOI:
10.1371/journal.pbio.3001231.r007
DOI:
10.1371/journal.pbio.3001231.r008
Language:
English
Publisher:
Public Library of Science (PLoS)
Publication Date:
2021
detail.hit.zdb_id:
2126773-X
Permalink