Language:

LetB Structure Reveals a Tunnel for Lipid Transport across the Bacterial Envelope

Cell, 2020-04, Vol.181 (3), p.653-664.e19 [Peer Reviewed Journal]

2020 Elsevier Inc. ;Copyright © 2020 Elsevier Inc. All rights reserved. ;ISSN: 0092-8674 ;EISSN: 1097-4172 ;DOI: 10.1016/j.cell.2020.03.030 ;PMID: 32359438

Full text available

Citations Cited by

Actions
1. Add to My Research
2. Remove from My Research
3. E-mail
4. Print
5. Permalink
6. Citation
7. EasyBib
8. EndNote
9. RefWorks
10. Delicious
11. Export RIS
12. Export BibTeX

Title:
LetB Structure Reveals a Tunnel for Lipid Transport across the Bacterial Envelope
Author: Isom, Georgia L. ; Coudray, Nicolas ; MacRae, Mark R. ; McManus, Collin T. ; Ekiert, Damian C. ; Bhabha, Gira
Subjects: bacteria ; bacterial cell envelope ; Bacterial Outer Membrane Proteins - metabolism ; Bacterial Proteins - metabolism ; Bacterial Proteins - physiology ; Biological Transport ; Cell Membrane - metabolism ; conformational dynamics ; cryo-EM ; Escherichia coli - metabolism ; Escherichia coli Proteins - metabolism ; LetB ; lipid transport ; Lipopolysaccharides - metabolism ; MCE ; membrane ; Membrane Proteins - metabolism ; Membrane Transport Proteins - metabolism ; microbiology ; Phospholipids - metabolism ; Protein Transport - physiology ; YebT
Is Part Of: Cell, 2020-04, Vol.181 (3), p.653-664.e19
Description: Gram-negative bacteria are surrounded by an outer membrane composed of phospholipids and lipopolysaccharide, which acts as a barrier and contributes to antibiotic resistance. The systems that mediate phospholipid trafficking across the periplasm, such as MCE (Mammalian Cell Entry) transporters, have not been well characterized. Our ~3.5 Å cryo-EM structure of the E. coli MCE protein LetB reveals an ~0.6 megadalton complex that consists of seven stacked rings, with a central hydrophobic tunnel sufficiently long to span the periplasm. Lipids bind inside the tunnel, suggesting that it functions as a pathway for lipid transport. Cryo-EM structures in the open and closed states reveal a dynamic tunnel lining, with implications for gating or substrate translocation. Our results support a model in which LetB establishes a physical link between the two membranes and creates a hydrophobic pathway for the translocation of lipids across the periplasm. [Display omitted] •Cryo-EM structures of LetB reveal a tunnel that spans the bacterial cell envelope•Lipids bind inside the tunnel, supporting a role for LetB in lipid transport•Different conformations reveal tunnel dynamics, with implications for transport Structures of the open and closed states of LetB reveal seven stacked rings that span between the two membranes of Gram-negative bacteria to facilitate lipid transport through the central tunnel.
Publisher: United States: Elsevier Inc
Language: English
Identifier: ISSN: 0092-8674
EISSN: 1097-4172
DOI: 10.1016/j.cell.2020.03.030
PMID: 32359438
Source: Cell Press Free Archives
MEDLINE

Back to results list


INSPIRE LIBRARY - TON DUC THANG UNIVERSITY	(84-028) 37 755 057	Feedback
19 Nguyen Huu Tho St. Dist.7, HCM	thuvien@tdtu.edu.vn	Feedback

LetB Structure Reveals a Tunnel for Lipid Transport across the Bacterial Envelope

2020 Elsevier Inc. ;Copyright © 2020 Elsevier Inc. All rights reserved. ;ISSN: 0092-8674 ;EISSN: 1097-4172 ;DOI: 10.1016/j.cell.2020.03.030 ;PMID: 32359438

Searching Remote Databases, Please Wait