DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lee HW | ko |
dc.contributor.author | Byun, Si Myung | ko |
dc.date.accessioned | 2013-03-03T13:27:42Z | - |
dc.date.available | 2013-03-03T13:27:42Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2003-08 | - |
dc.identifier.citation | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.307, no.4, pp.820 - 825 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | http://hdl.handle.net/10203/78873 | - |
dc.description.abstract | The autotransporter mode of surface presentation in Gram-negative bacteria requires a hypothetical C-terminal P-barrel which makes up an aqueous channel in the outer membrane. PaIA is a Pseudomonas sp. autotransporter lipolytic protein. PaIA is a 66 kDa protein that is composed of two parts, the N-terminal region (Ala(1)-Ala(296)) similar to the GDSL lipases and the C-terminal region (Leu(320)-Phe(612)) to the autotransporter. In this report, we provide biochemical and structural evidence demonstrating that the pore size of the P-barrel conduit is important in delivering the N-terminal domain to the cell surface. Among all the autotransporter domains two strictly conserved residues (Pro(478) and Gly(576) in PaIA) are converted to other various residues using site-directed mutagenesis. This investigation was made into the different pore-size mutants, affecting the folding of N-terminal domain. Wild P-domain contains a cavity of similar to2 mn diameter that is optimal for the active conformation of the N-terminal domains. However, deviation from the proper size of the pore, whether it is larger or smaller, is not suitable for the proper folding of the N-terminal catalytic domain. (C) 2003 Elsevier Inc. All rights reserved. | - |
dc.language | English | - |
dc.publisher | Academic Press Inc Elsevier Science | - |
dc.subject | TOXIN-B-SUBUNIT | - |
dc.subject | SINGLE-CHAIN FV | - |
dc.subject | ESCHERICHIA-COLI | - |
dc.subject | OUTER-MEMBRANE | - |
dc.subject | PSEUDOMONAS-AERUGINOSA | - |
dc.subject | BACTERIAL LIPASES | - |
dc.subject | LARGE CHANNELS | - |
dc.subject | IGA PROTEASE | - |
dc.subject | PROTEINS | - |
dc.subject | SECRETION | - |
dc.title | The pore size of the autotransporter domain is critical for the active translocation of the passenger domain | - |
dc.type | Article | - |
dc.identifier.wosid | 000184510100011 | - |
dc.identifier.scopusid | 2-s2.0-0038105549 | - |
dc.type.rims | ART | - |
dc.citation.volume | 307 | - |
dc.citation.issue | 4 | - |
dc.citation.beginningpage | 820 | - |
dc.citation.endingpage | 825 | - |
dc.citation.publicationname | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.contributor.nonIdAuthor | Lee HW | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | autotransporter | - |
dc.subject.keywordAuthor | pore size | - |
dc.subject.keywordAuthor | site-directed mutagenesis | - |
dc.subject.keywordAuthor | translocation | - |
dc.subject.keywordPlus | TOXIN-B-SUBUNIT | - |
dc.subject.keywordPlus | SINGLE-CHAIN FV | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | OUTER-MEMBRANE | - |
dc.subject.keywordPlus | PSEUDOMONAS-AERUGINOSA | - |
dc.subject.keywordPlus | BACTERIAL LIPASES | - |
dc.subject.keywordPlus | LARGE CHANNELS | - |
dc.subject.keywordPlus | IGA PROTEASE | - |
dc.subject.keywordPlus | PROTEINS | - |
dc.subject.keywordPlus | SECRETION | - |
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