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  An evolutionarily conserved glycine-tyrosine motif forms a folding core in outer membrane proteins.

Michalik, M., Orwick-Rydmark, M., Habeck, M., Alva, V., Arnold, T., & Linke, D. (2017). An evolutionarily conserved glycine-tyrosine motif forms a folding core in outer membrane proteins. PLoS One, 12(8): e0182016. doi:10.1371/journal.pone.0182016.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-D264-F Version Permalink: http://hdl.handle.net/21.11116/0000-0001-3AF2-D
Genre: Journal Article

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Michalik, M., Author
Orwick-Rydmark, M., Author
Habeck, M.1, Author              
Alva, V., Author
Arnold, T., Author
Linke, D., Author
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1Research Group of Statistical Inverse-Problems in Biophysics, MPI for Biophysical Chemistry, Max Planck Society, ou_1113580              

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 Abstract: An intimate interaction between a pair of amino acids, a tyrosine and glycine on neighboring beta-strands, has been previously reported to be important for the structural stability of auto-transporters. Here, we show that the conservation of this interacting pair extends to nearly all major families of outer membrane beta-barrel proteins, which are thought to have originated through duplication events involving an ancestral beta beta hairpin. We analyzed the function of this motif using the prototypical outer membrane protein OmpX. Stopped-flow fluorescence shows that two folding processes occur in the millisecond time regime, the rates of which are reduced in the tyrosine mutant. Folding assays further demonstrate a reduction in the yield of folded protein for the mutant compared to the wild-type, as well as a reduction in thermal stability. Taken together, our data support the idea of an evolutionarily conserved 'folding core' that affects the folding, membrane insertion, and thermal stability of outer membrane protein beta-barrels.

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Language(s): eng - English
 Dates: 2017-08-03
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.1371/journal.pone.0182016
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Title: PLoS One
Source Genre: Journal
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Pages: 24 Volume / Issue: 12 (8) Sequence Number: e0182016 Start / End Page: - Identifier: -