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Crystal structure of UbiX, an aromatic acid decarboxylase from the psychrophilic bacterium Colwellia psychrerythraea that undergoes FMN-induced conformational changes

Cited 11 time in wos
Cited 13 time in scopus

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dc.contributor.authorDo, Hackwon-
dc.contributor.authorLee, Jun Hyuck-
dc.contributor.authorHaJeung Park-
dc.contributor.authorPark, Hyun-
dc.contributor.authorHo Min Kim-
dc.contributor.authorHyun Ho Park-
dc.contributor.authorKim, Han-Woo-
dc.contributor.authorLee, Chang Woo-
dc.contributor.authorSoo Jin Kim-
dc.date.accessioned2018-03-29T06:04:14Z-
dc.date.available2018-03-29T06:04:14Z-
dc.date.issued2015-
dc.identifier.urihttps://repository.kopri.re.kr/handle/201206/7323-
dc.description.abstractThe 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.languageEnglish-
dc.titleCrystal structure of UbiX, an aromatic acid decarboxylase from the psychrophilic bacterium Colwellia psychrerythraea that undergoes FMN-induced conformational changes-
dc.title.alternative호냉성 박테리아인 Colwellia psychrerythraea 유래 UbiX 단백질의 FMN 결합에 의한 구조적 변화연구-
dc.typeArticle-
dc.identifier.bibliographicCitationDo, Hackwon, et al. 2015. "Crystal structure of UbiX, an aromatic acid decarboxylase from the psychrophilic bacterium Colwellia psychrerythraea that undergoes FMN-induced conformational changes". <em>SCIENTIFIC REPORTS</em>, 5(8196): 1-9.-
dc.citation.titleSCIENTIFIC REPORTS-
dc.citation.volume5-
dc.citation.number8196-
dc.identifier.doi10.1038/srep08196-
dc.citation.startPage1-
dc.citation.endPage9-
dc.description.articleClassificationSCIE-
dc.description.jcrRateJCR 2013:9.090909090909092-
dc.subject.keywordColwellia psychrerythraea-
dc.subject.keywordUbiX-
dc.subject.keywordX-ray crystallography-
dc.subject.keywordaromatic acid decarboxylase-
dc.subject.keywordubiquinone-
dc.identifier.localId2015-0003-
dc.identifier.scopusid2-s2.0-84938795067-
dc.identifier.wosid000348703200007-
Appears in Collections  
2014-2016, Antarctic Organisms: Cold-Adaptation Mechanism and Its Application (14-16) / Park; Hyun (PE14070; PE15070; PE16070)
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