Type 9 secretion system structures reveal a new protein transport mechanism

Type 9 secretion system structures reveal a new protein transport mechanism

The type 9 secretion system (T9SS) is the protein export pathway of bacteria of the Gram-negative Fibrobacteres–Chlorobi–Bacteroidetes superphylum and is an essential determinant of pathogenicity in severe periodontal disease. The central element of the T9SS is a so-far uncharacterized protein-condu...

Полное описание

Библиографические подробности
Главные авторы:	Lauber, F, Deme, J, Lea, S, Berks, B
Формат:	Journal article
Опубликовано:	Springer Nature 2018

Схожие документы

Structural insights into the mechanism of protein transport by the Type 9 Secretion System translocon
по: Lauber, F, и др.
Опубликовано: (2024)

Structure and mechanism of the proton-driven motor that powers Type 9 secretion and gliding motility
по: Hennell James, R, и др.
Опубликовано: (2021)

Core components of bacterial protein secretion systems revealed at high resolution by cryo-electron microscopy
по: Deme, J, и др.
Опубликовано: (2018)

Structure of a proton-powered molecular motor that drives protein transport and gliding motility
по: Berks, B, и др.
Опубликовано: (2020)

Structures of the Type IX Secretion/gliding motility motor from across the phylum Bacteroidetes
по: Hennell James, R, и др.
Опубликовано: (2022)

Structures of the Type IX Secretion/Gliding Motility Motor from across the Phylum Bacteroidetes
по: Rory Hennell James, и др.
Опубликовано: (2022-06-01)

New insights into the Tat protein transport cycle from characterising the assembled Tat translocon
по: Alcock, F, и др.
Опубликовано: (2022)

Three small partner proteins facilitate the type VII-dependent secretion of an antibacterial nuclease
по: Yaping Yang, и др.
Опубликовано: (2023-10-01)

Structure of the core of the type III secretion system export apparatus
по: Kuhlen, L, и др.
Опубликовано: (2018)

TatBC, TatB, and TatC form structurally autonomous units within the twin arginine protein transport system of Escherichia coli.
по: Orriss, G, и др.
Опубликовано: (2007)

The structure of an injectisome export gate demonstrates conservation of architecture in the core export gate between flagellar and virulence Type III secretion systems.
по: Johnson, S, и др.
Опубликовано: (2019)

Substrate-engaged type III secretion system structures reveal gating mechanism for unfolded protein translocation
по: Sean Miletic, и др.
Опубликовано: (2021-03-01)

Structures of the Shigella flexneri type 3 secretion system protein MxiC reveal conformational variability amongst homologues.
по: Deane, J, и др.
Опубликовано: (2008)

Structural analysis of substrate binding by the TatBC component of the twin-arginine protein transport system.
по: Tarry, M, и др.
Опубликовано: (2009)

Revealing the mechanisms of membrane protein export by virulence-associated bacterial secretion systems
по: Lea Krampen, и др.
Опубликовано: (2018-08-01)

Crystal structure of the Bacillus subtilis phosphodiesterase PhoD reveals an iron and calcium-containing active site.
по: Rodriguez, F, и др.
Опубликовано: (2014)

The DNA transporter ComEC has metal-dependent nuclease activity that is important for natural transformation
по: Silale, A, и др.
Опубликовано: (2021)

The Structure of an Injectisome Export Gate Demonstrates Conservation of Architecture in the Core Export Gate between Flagellar and Virulence Type III Secretion Systems
по: Steven Johnson, и др.
Опубликовано: (2019-06-01)

T9GPred: A Comprehensive Computational Tool for the Prediction of Type 9 Secretion System, Gliding Motility, and the Associated Secreted Proteins
по: Ajaya Kumar Sahoo, и др.
Опубликовано: (2023-09-01)

Precursor-receptor interactions in the twin arginine protein transport pathway probed with a new receptor complex preparation
по: Wojnowska, M, и др.
Опубликовано: (2018)

<it>Yersinia enterocolitica </it>type III secretion: Evidence for the ability to transport proteins that are folded prior to secretion
по: Neumayer Wibke, и др.
Опубликовано: (2004-07-01)

Structural model for the protein-translocating element of the twin-arginine transport system.
по: Rodriguez, F, и др.
Опубликовано: (2013)

Symmetry mismatch in the MS-ring of the bacterial flagellar rotor explains the structural coordination of secretion and rotation
по: Johnson, S, и др.
Опубликовано: (2020)

A Novel Mechanism for Protein Delivery by the Type 3 Secretion System for Extracellularly Secreted Proteins
по: Farid Tejeda-Dominguez, и др.
Опубликовано: (2017-05-01)

A signal sequence suppressor mutant that stabilizes an assembled state of the twin arginine translocase
по: Huang, Q, и др.
Опубликовано: (2017)

Structural insights into the control of type three secretion
по: Abrusci, P, и др.
Опубликовано: (2011)

Structure of the TatC core of the twin-arginine protein transport system.
по: Rollauer, SE, и др.
Опубликовано: (2012)

Structure of the TatC core of the twin-arginine protein transport system
по: Rollauer, SE, и др.
Опубликовано: (2012)

Structural basis for antibiotic transport and inhibition in PepT2
по: Parker, JL, и др.
Опубликовано: (2024)

Structures of the stator complex that drives rotation of the bacterial flagellum
по: Deme, J, и др.
Опубликовано: (2020)

The substrate specificity switch FlhB assembles onto the export gate to regulate type three secretion
по: Kuhlen, L, и др.
Опубликовано: (2020)

The chlamydial type III secretion mechanism: Revealing cracks in a tough nut
по: Helen Jennifer Betts-Hampikian, и др.
Опубликовано: (2010-10-01)

Structure and function of bacterial proteins secreted by the type three secretion and twin arginine translocation pathways
по: Lillington, J, и др.
Опубликовано: (2011)

Aberrant topologies of bacterial membrane proteins revealed by high sensitivity fluorescence labelling
по: Hickman, SJ, и др.
Опубликовано: (2023)

Structural basis for specificity and promiscuity in a carrier protein/enzyme system from the sulfur cycle
по: Grabarczyk, DB, и др.
Опубликовано: (2015)

Aequorea's secrets revealed: New fluorescent proteins with unique properties for bioimaging and biosensing.
по: Gerard G Lambert, и др.
Опубликовано: (2020-11-01)

Structural and functional studies on the N-terminal domain of the Shigella type III secretion protein MxiG.
по: McDowell, M, и др.
Опубликовано: (2011)

Structural and Functional Studies on the N-terminal Domain of the Shigella Type III Secretion Protein MxiG
по: McDowell, M, и др.
Опубликовано: (2011)

Helical structure of the needle of the type III secretion system of Shigella flexneri.
по: Cordes, F, и др.
Опубликовано: (2003)

Revealing the secrets of secretion
по: Antony Galione, и др.
Опубликовано: (2018-11-01)