Omp85Tt from Thermus thermophilus HB27 : an ancestral type of the Omp85 protein family

Nesper, Jutta and Brosig, Alexander and Ringler, Philippe and Patel, Geetika J. and Müller, Shirley A. and Kleinschmidt, Joerg H. and Boos, Winfried and Diederichs, Kay and Welte, Wolfram. (2008) Omp85Tt from Thermus thermophilus HB27 : an ancestral type of the Omp85 protein family. Journal of bacteriology, Vol. 190, H. 13. pp. 4568-4575.

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Official URL: http://edoc.unibas.ch/dok/A5262463

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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 compn. nor much about integral membrane proteins is known. The genome of HB27 encodes one Omp85-like protein, Omp85Tt, representing an ancestral type of this family. We overexpressed Omp85Tt in T. thermophilus and purified it from the native outer membranes. In the presence of detergent, purified Omp85Tt existed mainly as a monomer, composed of two stable protease-resistant modules. CD spectroscopy indicated predominantly beta -sheet secondary structure. Electron microscopy of neg. stained lipid-embedded Omp85Tt revealed ring-like structures with a central cavity of .apprx.1.5 nm in diam. Single-channel conductance recordings indicated that Omp85Tt forms ion channels with two different conducting states, characterized by conductances of .apprx.0.4 nS and .apprx.0.65 nS, resp. [on SciFinder (R)]
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Engel)
UniBasel Contributors:Müller, Shirley and Ringler, Philippe
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:American Society for Microbiology
Note:Publication type according to Uni Basel Research Database: Journal article
Last Modified:22 Mar 2012 14:23
Deposited On:22 Mar 2012 13:32

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