Zobrazeno 1 - 10
of 104
pro vyhledávání: '"Harris D, Bernstein"'
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-15 (2024)
Abstract The translocation and assembly module (TAM) has been proposed to play a crucial role in the assembly of a small subset of outer membrane proteins (OMPs) in Proteobacteria based on experiments conducted in vivo using tamA and tamB mutant stra
Externí odkaz:
https://doaj.org/article/f16dae8ac5b74630aff73f288299dd2a
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-14 (2024)
Abstract Members of the Omp85 superfamily of outer membrane proteins (OMPs) found in Gram-negative bacteria, mitochondria and chloroplasts are characterized by a distinctive 16-stranded β-barrel transmembrane domain and at least one periplasmic POTR
Externí odkaz:
https://doaj.org/article/396aa9efafe945a9933a64c7527759d5
Publikováno v:
mBio, Vol 13, Iss 5 (2022)
ABSTRACT Several antibacterial compounds have recently been discovered that potentially inhibit the activity of BamA, an essential subunit of a heterooligomer (the barrel assembly machinery or BAM) that assembles outer membrane proteins (OMPs) in Gra
Externí odkaz:
https://doaj.org/article/d625f4d5d3314cf8a9a8230186b84a29
Publikováno v:
mBio, Vol 12, Iss 4 (2021)
ABSTRACT Many integral membrane proteins form oligomeric complexes, but the assembly of these structures is poorly understood. Here, we show that the assembly of OmpC, a trimeric porin that resides in the Escherichia coli outer membrane (OM), can be
Externí odkaz:
https://doaj.org/article/3f17073ab5a14460aaa1a4fbf2b865b9
Autor:
Matthew T. Doyle, Harris D. Bernstein
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-13 (2019)
The integration of β-barrel proteins into the bacterial outer membrane (OM) is catalysed by the β-barrel assembly machinery (BAM). Here authors develop a method to trap an E. coli β-barrel protein bound stably to BamA at a late stage of assembly i
Externí odkaz:
https://doaj.org/article/7ee3ebed676f43cab7020c8070468411
Publikováno v:
mBio, Vol 12, Iss 3 (2021)
Proteins that are embedded in the outer membrane of Gram-negative bacteria (OMPs) play an important role in protecting the cell from harmful chemicals. OMPs share a architecture and often contain a conserved sequence motif (β motif) of unknown funct
Externí odkaz:
https://doaj.org/article/2616f31e2e3f4d2685e3e8ede7c9bb1e
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-12 (2017)
The Bam complex promotes the insertion of β-barrel proteins (such as UpaG, a trimeric autotransporter adhesin) into the bacterial outer membrane. Here, Sikdar et al. show that UpaG β-barrel segments fold into a trimeric structure in the periplasm b
Externí odkaz:
https://doaj.org/article/e236f41f66004aaf9d50b8a6a3698135
Autor:
Rakesh Sikdar, Harris D. Bernstein
Publikováno v:
mBio, Vol 10, Iss 5 (2019)
ABSTRACT Trimeric autotransporter adhesins (TAAs) are a family of bacterial outer membrane (OM) proteins that are comprised of three identical subunits. Each subunit contains an N-terminal extracellular (“passenger”) domain and a short C-terminal
Externí odkaz:
https://doaj.org/article/043d320418494428bead6e4249e9f957
Members of the Omp85 superfamily of outer membrane proteins (OMPs) found in Gram-negative bacteria, mitochondria and chloroplasts are characterized by a distinctive 16-stranded β-barrel transmembrane domain and at least one periplasmic POTRA domain.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5112ced1ecd0354fff696958c3a7c211
https://doi.org/10.1101/2023.04.17.537245
https://doi.org/10.1101/2023.04.17.537245
Autor:
Renuka Kudva, Pengfei Tian, Fátima Pardo-Avila, Marta Carroni, Robert B Best, Harris D Bernstein, Gunnar von Heijne
Publikováno v:
eLife, Vol 7 (2018)
The E. coli ribosome exit tunnel can accommodate small folded proteins, while larger ones fold outside. It remains unclear, however, to what extent the geometry of the tunnel influences protein folding. Here, using E. coli ribosomes with deletions in
Externí odkaz:
https://doaj.org/article/b8a00e7659374bc399c67af75ad5de29