| pubmed-article:16549796 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16549796 | lifeskim:mentions | umls-concept:C0036536 | lld:lifeskim |
| pubmed-article:16549796 | lifeskim:mentions | umls-concept:C0036537 | lld:lifeskim |
| pubmed-article:16549796 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:16549796 | lifeskim:mentions | umls-concept:C0185026 | lld:lifeskim |
| pubmed-article:16549796 | lifeskim:mentions | umls-concept:C0205214 | lld:lifeskim |
| pubmed-article:16549796 | lifeskim:mentions | umls-concept:C1705535 | lld:lifeskim |
| pubmed-article:16549796 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:16549796 | lifeskim:mentions | umls-concept:C0136166 | lld:lifeskim |
| pubmed-article:16549796 | pubmed:issue | 13 | lld:pubmed |
| pubmed-article:16549796 | pubmed:dateCreated | 2006-3-29 | lld:pubmed |
| pubmed-article:16549796 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16549796 | pubmed:abstractText | Many virulence factors secreted from pathogenic Gram-negative bacteria are autotransporter proteins. The final step of autotransporter secretion is C --> N-terminal threading of the passenger domain through the outer membrane (OM), mediated by a cotranslated C-terminal porin domain. The native structure is formed only after this final secretion step, which requires neither ATP nor a proton gradient. Sequence analysis reveals that, despite size, sequence, and functional diversity among autotransporter passenger domains, >97% are predicted to form parallel beta-helices, indicating this structural topology may be important for secretion. We report the folding behavior of pertactin, an autotransporter passenger domain from Bordetella pertussis. The pertactin beta-helix folds reversibly in isolation, but folding is much slower than expected based on size and native-state topology. Surprisingly, pertactin is not prone to aggregation during folding, even though folding is extremely slow. Interestingly, equilibrium denaturation results in the formation of a partially folded structure, a stable core comprising the C-terminal half of the protein. Examination of the pertactin crystal structure does not reveal any obvious reason for the enhanced stability of the C terminus. In vivo, slow folding would prevent premature folding of the passenger domain in the periplasm, before OM secretion. Moreover, the extra stability of the C-terminal rungs of the beta-helix might serve as a template for the formation of native protein during OM secretion; hence, vectorial folding of the beta-helix could contribute to the energy-independent translocation mechanism. Coupled with the sequence analysis, the results presented here suggest a general mechanism for autotransporter secretion. | lld:pubmed |
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| pubmed-article:16549796 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16549796 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16549796 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16549796 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16549796 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:16549796 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:16549796 | pubmed:author | pubmed-author:BergerBonnieB | lld:pubmed |
| pubmed-article:16549796 | pubmed:author | pubmed-author:ClarkPatricia... | lld:pubmed |
| pubmed-article:16549796 | pubmed:author | pubmed-author:McDonnellAndr... | lld:pubmed |
| pubmed-article:16549796 | pubmed:author | pubmed-author:JunkerMircoM | lld:pubmed |
| pubmed-article:16549796 | pubmed:author | pubmed-author:SchusterChris... | lld:pubmed |
| pubmed-article:16549796 | pubmed:author | pubmed-author:SorgKelli AKA | lld:pubmed |
| pubmed-article:16549796 | pubmed:author | pubmed-author:FinnMary CMC | lld:pubmed |
| pubmed-article:16549796 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16549796 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:16549796 | pubmed:volume | 103 | lld:pubmed |
| pubmed-article:16549796 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16549796 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16549796 | pubmed:pagination | 4918-23 | lld:pubmed |
| pubmed-article:16549796 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:16549796 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16549796 | pubmed:articleTitle | Pertactin beta-helix folding mechanism suggests common themes for the secretion and folding of autotransporter proteins. | lld:pubmed |
| pubmed-article:16549796 | pubmed:affiliation | Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46556-5670, USA. | lld:pubmed |
| pubmed-article:16549796 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16549796 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:16549796 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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