Article
|
Open Access
Featured
-
-
Article |
SlyB encapsulates outer membrane proteins in stress-induced lipid nanodomains
SlyB, a lipoprotein in the PhoPQ stress regulon in Gram-negative bacteria, forms stable stress-induced complexes with the outer membrane proteome.
- Arne Janssens
- , Van Son Nguyen
- & Han Remaut
-
Article |
Single-molecule dynamics show a transient lipopolysaccharide transport bridge
As well as being the substrate for the lipopolysaccharide transport protein complex comprising LptA–G, lipopolysaccharide binding to Lpt proteins promotes their assembly into a bridge linking the inner and outer membranes of Gram-negative bacteria.
- Lisa Törk
- , Caitlin B. Moffatt
- & Daniel Kahne
-
Article |
Structure of an endogenous mycobacterial MCE lipid transporter
Proteins of the Mycobacterium smegmatis Mce1 system assemble to form an elongated ABC transporter complex that is long enough to span the impermeable mycobacterial cell envelope.
- James Chen
- , Alice Fruhauf
- & Damian C. Ekiert
-
Article
| Open Access
Structural basis of NINJ1-mediated plasma membrane rupture in cell death
Structural, biochemical and mutagenesis studies indicate that, in dying cells, the membrane protein NINJ1 assembles into filaments, disrupting the cell membrane.
- Morris Degen
- , José Carlos Santos
- & Sebastian Hiller
-
Article
| Open Access
Peptidoglycan maturation controls outer membrane protein assembly
Peptidoglycan stem peptides in the Gram-negative bacterial cell wall regulate the insertion of essential outer membrane proteins, thus representing a potential target for antibiotic design.
- Gideon Mamou
- , Federico Corona
- & Waldemar Vollmer
-
Article |
Architecture and assembly mechanism of native glycine receptors
Cryo-electron microscopy structures of pig glycine receptors indicate that they are predominantly assembled with 4α:1β stoichiometry via α-homotrimer and homotetramer intermediates.
- Hongtao Zhu
- & Eric Gouaux
-
Article
| Open Access
Structural basis of GABAB receptor–Gi protein coupling
Cryo-electron microscopy structure of heterodimeric GABAB receptor in complex with Gi1 protein reveals that the mode of G-protein binding in this class-C G-protein-coupled receptor differs from that of other classes.
- Cangsong Shen
- , Chunyou Mao
- & Jianfeng Liu
-
Article |
The antibiotic darobactin mimics a β-strand to inhibit outer membrane insertase
Structural studies resolve how the antibiotic darobactin inhibits the bacterial BAM insertase.
- Hundeep Kaur
- , Roman P. Jakob
- & Sebastian Hiller
-
Article |
Computational design of transmembrane pores
An approach for the design of protein pores is demonstrated by the computational design and subsequent experimental expression of both an ion-selective and a large transmembrane pore.
- Chunfu Xu
- , Peilong Lu
- & David Baker
-
Article |
LEM2 phase separation promotes ESCRT-mediated nuclear envelope reformation
Following cell division, phase separation of the transmembrane adaptor LEM2 ensures that the ESCRT machinery remodels microtubules and seals the nuclear envelope.
- Alexander von Appen
- , Dollie LaJoie
- & Adam Frost
-
Article |
Structure and autoregulation of a P4-ATPase lipid flippase
Cryo-EM structures of the yeast P4-ATPase Drs2p–Cdc50p in three different states of activation provide insights into the function of this lipid flippase, including mechanisms of autoinhibition and PI4P-dependent activation.
- Milena Timcenko
- , Joseph A. Lyons
- & Poul Nissen
-
Article |
Structure of native lens connexin 46/50 intercellular channels by cryo-EM
Cryo-electron microscopy structures of connexin channels composed of connexin 46 and connexin 50 in an open-state reveal features that govern permselectivity and the location of mutated residues linked to herediatry cataracts.
- Janette B. Myers
- , Bassam G. Haddad
- & Steve L. Reichow
-
Letter |
Cryo-EM of the dynamin polymer assembled on lipid membrane
A cryo-electron microscopy structure of human dynamin-1 demonstrates conformational changes and sheds light on the fission of membranes during endocytosis.
- Leopold Kong
- , Kem A. Sochacki
- & Jenny E. Hinshaw
-
Letter |
The outer membrane is an essential load-bearing element in Gram-negative bacteria
The outer membrane of Gram-negative bacteria is shown to be at least as stiff as the cell wall, and this property enables it to protect cells from mechanical pertubations.
- Enrique R. Rojas
- , Gabriel Billings
- & Kerwyn Casey Huang
-
Article |
Structural basis of mitochondrial receptor binding and constriction by DRP1
Cryo-electron microscopy is used to resolve the structure of human dynamin-related protein 1 co-assembled with its receptor mitochondrial dynamics protein of 49 kDa, along with an analysis of structure- and disease-based mutations.
- Raghav Kalia
- , Ray Yu-Ruei Wang
- & Adam Frost
-
Letter |
Reconstitution of the tubular endoplasmic reticulum network with purified components
In the presence of GTP, a tubular endoplasmic reticulum network can be reconstituted with only two purified membrane proteins.
- Robert E. Powers
- , Songyu Wang
- & Tom A. Rapoport
-
Letter |
MFN1 structures reveal nucleotide-triggered dimerization critical for mitochondrial fusion
Crystal structures of engineered human MFN1 in different stages of GTP hydrolysis provide insights into the GTP-induced conformational changes that promote MFN1 dimerization to bring about mitochondrial fusion.
- Yu-Lu Cao
- , Shuxia Meng
- & Song Gao
-
Letter |
Pore architecture of TRIC channels and insights into their gating mechanism
X-ray structures of C. elegans TRIC-B subtype channels reveal that the membrane proteins form a symmetrical homotrimeric complex, and a mechanistic model to explain the complex gating mechanism of TRIC channels is proposed.
- Hanting Yang
- , Miaohui Hu
- & Zhenfeng Liu
-
Letter |
X-ray structure of the human α4β2 nicotinic receptor
Nicotinic acetylcholine receptors are ligand-gated ion channels that mediate fast chemical neurotransmission; here, the first X-ray crystal structure of a nicotinic receptor is reported, revealing how nicotine stabilizes the receptor in a non-conducting, desensitized conformation.
- Claudio L. Morales-Perez
- , Colleen M. Noviello
- & Ryan E. Hibbs
-
Article |
Structural basis of outer membrane protein insertion by the BAM complex
Two crystal structures of the Escherichia coli β-barrel assembly machinery (BAM complex) are presented, one of which includes all five subunits (BamA–BamE), in two distinct conformational states; together with functional assays and molecular dynamics stimulations, these structures help to generate a model for outer membrane protein insertion.
- Yinghong Gu
- , Huanyu Li
- & Changjiang Dong
-
Letter |
Structure of a bacterial energy-coupling factor transporter
The crystal structure of a nucleotide-free energy-coupling factor transporter from Lactobacillus brevis at a resolution of 3.5 Å suggests a plausible working model for the transport cycle of such transporters.
- Tingliang Wang
- , Guobin Fu
- & Yigong Shi
-
Article |
The mechanism of membrane-associated steps in tail-anchored protein insertion
- Malaiyalam Mariappan
- , Agnieszka Mateja
- & Robert J. Keenan
Molecular insights into capsular polysaccharide secretion