Cargando…
Conserved Omp85 lid-lock structure and substrate recognition in FhaC
Omp85 proteins mediate translocation of polypeptide substrates across and into cellular membranes. They share a common architecture comprising substrate-interacting POTRA domains, a C-terminal 16-stranded β-barrel pore and two signature motifs located on the inner barrel wall and at the tip of the e...
Autores principales: | Maier, Timm, Clantin, Bernard, Gruss, Fabian, Dewitte, Frédérique, Delattre, Anne-Sophie, Jacob-Dubuisson, Françoise, Hiller, Sebastian, Villeret, Vincent |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Pub. Group
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4490367/ https://www.ncbi.nlm.nih.gov/pubmed/26058369 http://dx.doi.org/10.1038/ncomms8452 |
Ejemplares similares
-
Large-Scale Conformational Changes of FhaC Provide Insights Into the Two-Partner Secretion Mechanism
por: Sicoli, Giuseppe, et al.
Publicado: (2022) -
Structural insights into ChpT, an essential dimeric histidine phosphotransferase regulating the cell cycle in Caulobacter crescentus
por: Fioravanti, Antonella, et al.
Publicado: (2012) -
Crystal structure of human Mediator subunit MED23
por: Monté, Didier, et al.
Publicado: (2018) -
Omp85 from the Thermophilic Cyanobacterium Thermosynechococcus elongatus Differs from Proteobacterial Omp85 in Structure and Domain Composition
por: Arnold, Thomas, et al.
Publicado: (2010) -
Requirements for the import of neisserial Omp85 into the outer membrane of human mitochondria
por: Ott, Christine, et al.
Publicado: (2013)