ArticleJournal of bacteriology2008
Omp85(Tt) from Thermus thermophilus HB27: an ancestral type of the Omp85 protein family.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- The Formation ofMembranes · 2023Article
- Inward-facing glycine residues create sharp turns in β-barrel membrane proteins.Biochimica et biophysica acta. Biomembranes · 2021Article
- ProLIF - quantitative integrin protein-protein interactions and synergistic membrane effects on proteoliposomes.Journal of cell science · 2018Article
- Article
- A tamB homolog is involved in maintenance of cell envelope integrity and stress resistance of Deinococcus radiodurans.Scientific reports · 2017Article
- Evolution of the Translocation and Assembly Module (TAM).Genome biology and evolution · 2015Article
- TtOmp85, a β-barrel assembly protein, functions by barrel augmentation.Biochemistry · 2015Article
- The β-barrel assembly machinery (BAM) is required for the assembly of a primitive S-layer protein in the ancient outer membrane of Thermus thermophilus.Extremophiles : life under extreme conditions · 2012Article
- Homogeneous incorporation of secondary cell wall polysaccharides to the cell wall of Thermus thermophilus HB27.Extremophiles : life under extreme conditions · 2012Article
- Unusual N-terminal ααβαββα fold of PilQ from Thermus thermophilus mediates ring formation and is essential for piliation.The Journal of biological chemistry · 2012Article
- Assembly of the β-Barrel Outer Membrane Proteins in Gram-Negative Bacteria, Mitochondria, and Chloroplasts.ISRN molecular biology · 2012Review
- TP0326, a Treponema pallidum β-barrel assembly machinery A (BamA) orthologue and rare outer membrane protein.Molecular microbiology · 2011Article
- Omp85 from the thermophilic cyanobacterium Thermosynechococcus elongatus differs from proteobacterial Omp85 in structure and domain composition.The Journal of biological chemistry · 2010Article
- Biogenesis of beta-barrel membrane proteins in bacteria and eukaryotes: evolutionary conservation and divergence.Cellular and molecular life sciences : CMLS · 2009Review
- Thermus thermophilus as biological model.Extremophiles : life under extreme conditions · 2009Review
- Expression, crystallization and preliminary X-ray analysis of an outer membrane protein from Thermus thermophilus HB27.Acta crystallographica. Section F, Structural biology and crystallization communications · 2008Article
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteins belonging to the Omp85 family are involved in the assembly of beta-barrel outer membrane proteins or in the translocation of proteins across the outer membrane in bacteria, mitochondria, and chloroplasts. The cell envelope of the thermophilic bacterium Thermus thermophilus HB27 is multilayered, including an outer membrane that is not well characterized. Neither the precise lipid composition nor much about integral membrane proteins is known. The genome of HB27 encodes one Omp85-like protein, Omp85(Tt), representing an ancestral type of this family. We overexpressed Omp85(Tt) in T. thermophilus and purified it from the native outer membranes. In the presence of detergent, purified Omp85(Tt) existed mainly as a monomer, composed of two stable protease-resistant modules. Circular dichroism spectroscopy indicated predominantly beta-sheet secondary structure. Electron microscopy of negatively stained lipid-embedded Omp85(Tt) revealed ring-like structures with a central cavity of approximately 1.5 nm in diameter. Single-channel conductance recordings indicated that Omp85(Tt) forms ion channels with two different conducting states, characterized by conductances of approximately 0.4 nS and approximately 0.65 nS, respectively.
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