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Purification, crystallization, and preliminary X-ray crystallographic studies of FMN-bound and FMN-free forms of aromatic acid decarboxylase (CpsUbiX) from the psychrophilic bacterium Colwellia psychrerythraea 34H

Cited 3 time in wos
Cited 3 time in scopus

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dc.contributor.authorLee, Jun Hyuck-
dc.contributor.authorKim, Hak Jun-
dc.contributor.authorDo, Hackwon-
dc.contributor.authorLee, Chang Woo-
dc.contributor.authorHan, Se Jong-
dc.contributor.authorLee, Sung Gu-
dc.contributor.authorPark, Hyun-
dc.date.accessioned2018-03-29T05:59:23Z-
dc.date.available2018-03-29T05:59:23Z-
dc.date.issued2014-
dc.identifier.urihttps://repository.kopri.re.kr/handle/201206/7251-
dc.description.abstractThe ubiX gene (UniProtKB code Q489U8) of Colwellia psychrerythraea strain 34H has been annotated as a putative flavin mononucleotide- (FMN-) dependent aromatic acid decarboxylase. Based on previous studies of homologous proteins, CpsUbiX is thought to catalyze the decarboxylation of 3-octaprenyl-4-hydroxybenzoate to produce 2-polyprenylphenol in the ubiquinone biosynthesis pathway using a noncovalently bound FMN molecule as a cofactor. However, the detailed mechanisms of this important enzyme are not yet clear and need to be further elucidated. In this study, we found that the V47S single mutation resulted in a loss of FMN binding, resulting in the production of the FMN-free CpsUbiX protein. This mutation likely destabilizes FMN-protein interactions without affecting overall structural folding. To fully characterize the conformational changes upon FMN binding and enzymatic mechanism at the molecular level, the wild-type (FMN-bound) and V47S mutant (FMN-free) CpsUbiX proteins were purified and crystallized using the sitting-drop vapor diffusion method. Furthermore, complete diffraction data sets of FMN-bound (space group C2221) and FMN-free (space group P23) forms were obtained to 2.0 and 1.76 A resolution, respectively.-
dc.languageEnglish-
dc.titlePurification, crystallization, and preliminary X-ray crystallographic studies of FMN-bound and FMN-free forms of aromatic acid decarboxylase (CpsUbiX) from the psychrophilic bacterium Colwellia psychrerythraea 34H-
dc.title.alternative호냉성 박테리아인 Colwellia psychrerythraea 34H 유래 aromatic acid decarboxylase (CpsUbiX) 단백질의 정제, 결정화 및 X-선 결정학적 연구-
dc.typeArticle-
dc.identifier.bibliographicCitationLee, Jun Hyuck, et al. 2014. "Purification, crystallization, and preliminary X-ray crystallographic studies of FMN-bound and FMN-free forms of aromatic acid decarboxylase (CpsUbiX) from the psychrophilic bacterium Colwellia psychrerythraea 34H". <em>Acta Crystallographica Section F: Structural Biology Communications</em>, 70: 215-220.-
dc.citation.titleActa Crystallographica Section F: Structural Biology Communications-
dc.citation.volume70-
dc.identifier.doi10.1107/S2053230X1303447X-
dc.citation.startPage215-
dc.citation.endPage220-
dc.description.articleClassificationSCIE-
dc.description.jcrRateJCR 2012:95.862-
dc.subject.keyword3-octaprenyl-4-hydroxybenzoate carboxy-lyase-
dc.subject.keywordAromatic acid decarboxylase-
dc.subject.keywordColwellia psychrerythraea 34H-
dc.subject.keywordX-ray crystallography-
dc.identifier.localId2014-0004-
dc.identifier.scopusid2-s2.0-84905489596-
dc.identifier.wosid000332229200015-
Appears in Collections  
2013-2013, Planning research for the practical application of antifreeze protein (13-13) / Lee, Sung Gu (PE13270)
2014-2016, Antarctic Organisms: Cold-Adaptation Mechanism and Its Application (14-16) / Park; Hyun (PE14070; PE15070; PE16070)
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