DC Field | Value | Language |
---|---|---|
dc.contributor.author | Hackwon, Do | ko |
dc.contributor.author | Kim, Soo Jin | ko |
dc.contributor.author | Lee, Chang Woo | ko |
dc.contributor.author | Kim, Han-Woo | ko |
dc.contributor.author | Park, Hyun Ho | ko |
dc.contributor.author | Kim, Ho-Min | ko |
dc.contributor.author | Park, Hyun | ko |
dc.contributor.author | Park, HaJeung | ko |
dc.contributor.author | Lee, Jun Hyuck | ko |
dc.date.accessioned | 2015-04-08T04:21:44Z | - |
dc.date.available | 2015-04-08T04:21:44Z | - |
dc.date.created | 2015-02-21 | - |
dc.date.created | 2015-02-21 | - |
dc.date.created | 2015-02-21 | - |
dc.date.issued | 2015-02 | - |
dc.identifier.citation | SCIENTIFIC REPORTS, v.5 | - |
dc.identifier.issn | 2045-2322 | - |
dc.identifier.uri | http://hdl.handle.net/10203/195522 | - |
dc.description.abstract | The ubiX gene of Colwellia psychrerythraea strain 34H encodes a 3-octaprenyl-4-hydroxybenzoate carboxylase (CpsUbiX, UniProtKB code: Q489U8) that is involved in the third step of the ubiquinone biosynthesis pathway and harbors a flavin mononucleotide (FMN) as a potential cofactor. Here, we report the crystal structures of two forms of CpsUbiX: an FMN-bound wild type form and an FMN-unbound V47S mutant form. CpsUbiX is a dodecameric enzyme, and each monomer possesses a typical Rossmann-fold structure. The FMN-binding domain of UbiX is composed of three neighboring subunits. The highly conserved Gly15, Ser41, Val47, and Tyr171 residues play important roles in FMN binding. Structural comparison of the FMN-bound wild type form with the FMN-free form reveals a significant conformational difference in the C-terminal loop region (comprising residues 170-176 and 195-206). Subsequent computational modeling and liposome binding assay both suggest that the conformational flexibility observed in the C-terminal loops plays an important role in substrate and lipid bindings. The crystal structures presented in this work provide structural framework and insights into the catalytic mechanism of CpsUbiX. | - |
dc.language | English | - |
dc.publisher | NATURE PUBLISHING GROUP | - |
dc.subject | UBIQUINONE BIOSYNTHESIS | - |
dc.subject | MOLECULAR-DYNAMICS | - |
dc.subject | ESCHERICHIA-COLI | - |
dc.subject | PROTEIN | - |
dc.subject | PROGRAM | - |
dc.subject | MODEL | - |
dc.title | Crystal structure of UbiX, an aromatic acid decarboxylase from the psychrophilic bacterium Colwellia psychrerythraea that undergoes FMN-induced conformational changes | - |
dc.type | Article | - |
dc.identifier.wosid | 000348703200007 | - |
dc.identifier.scopusid | 2-s2.0-84938795067 | - |
dc.type.rims | ART | - |
dc.citation.volume | 5 | - |
dc.citation.publicationname | SCIENTIFIC REPORTS | - |
dc.identifier.doi | 10.1038/srep08196 | - |
dc.contributor.localauthor | Kim, Ho-Min | - |
dc.contributor.nonIdAuthor | Hackwon, Do | - |
dc.contributor.nonIdAuthor | Lee, Chang Woo | - |
dc.contributor.nonIdAuthor | Kim, Han-Woo | - |
dc.contributor.nonIdAuthor | Park, Hyun Ho | - |
dc.contributor.nonIdAuthor | Park, Hyun | - |
dc.contributor.nonIdAuthor | Park, HaJeung | - |
dc.contributor.nonIdAuthor | Lee, Jun Hyuck | - |
dc.description.isOpenAccess | Y | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | UBIQUINONE BIOSYNTHESIS | - |
dc.subject.keywordPlus | MOLECULAR-DYNAMICS | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | PROGRAM | - |
dc.subject.keywordPlus | MODEL | - |
dc.subject.keywordPlus | UBIQUINONE BIOSYNTHESIS | - |
dc.subject.keywordPlus | MOLECULAR-DYNAMICS | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | PROGRAM | - |
dc.subject.keywordPlus | MODEL | - |
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