An evolutionarily conserved glycine-tyrosine motif forms a folding core in outer membrane proteins.
An intimate interaction between a pair of amino acids, a tyrosine and glycine on neighboring β-strands, has been previously reported to be important for the structural stability of autotransporters. Here, we show that the conservation of this interacting pair extends to nearly all major families of...
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doaj-0ceb679875ca45818a1d4df7b61e7f442020-11-24T21:38:22ZengPublic Library of Science (PLoS)PLoS ONE1932-62032017-01-01128e018201610.1371/journal.pone.0182016An evolutionarily conserved glycine-tyrosine motif forms a folding core in outer membrane proteins.Marcin MichalikMarcella Orwick-RydmarkMichael HabeckVikram AlvaThomas ArnoldDirk LinkeAn intimate interaction between a pair of amino acids, a tyrosine and glycine on neighboring β-strands, has been previously reported to be important for the structural stability of autotransporters. Here, we show that the conservation of this interacting pair extends to nearly all major families of outer membrane β-barrel proteins, which are thought to have originated through duplication events involving an ancestral ββ 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 β-barrels.http://europepmc.org/articles/PMC5542473?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Marcin Michalik Marcella Orwick-Rydmark Michael Habeck Vikram Alva Thomas Arnold Dirk Linke |
spellingShingle |
Marcin Michalik Marcella Orwick-Rydmark Michael Habeck Vikram Alva Thomas Arnold Dirk Linke An evolutionarily conserved glycine-tyrosine motif forms a folding core in outer membrane proteins. PLoS ONE |
author_facet |
Marcin Michalik Marcella Orwick-Rydmark Michael Habeck Vikram Alva Thomas Arnold Dirk Linke |
author_sort |
Marcin Michalik |
title |
An evolutionarily conserved glycine-tyrosine motif forms a folding core in outer membrane proteins. |
title_short |
An evolutionarily conserved glycine-tyrosine motif forms a folding core in outer membrane proteins. |
title_full |
An evolutionarily conserved glycine-tyrosine motif forms a folding core in outer membrane proteins. |
title_fullStr |
An evolutionarily conserved glycine-tyrosine motif forms a folding core in outer membrane proteins. |
title_full_unstemmed |
An evolutionarily conserved glycine-tyrosine motif forms a folding core in outer membrane proteins. |
title_sort |
evolutionarily conserved glycine-tyrosine motif forms a folding core in outer membrane proteins. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2017-01-01 |
description |
An intimate interaction between a pair of amino acids, a tyrosine and glycine on neighboring β-strands, has been previously reported to be important for the structural stability of autotransporters. Here, we show that the conservation of this interacting pair extends to nearly all major families of outer membrane β-barrel proteins, which are thought to have originated through duplication events involving an ancestral ββ 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 β-barrels. |
url |
http://europepmc.org/articles/PMC5542473?pdf=render |
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