Crystal structure of oleate hydratase from Stenotrophomonas sp KCTC 12332 reveals conformational plasticity surrounding the FAD binding site
DC Field | Value | Language |
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dc.contributor.author | Park, Ae Kyung | - |
dc.contributor.author | Lee, Gyeong Hweon | - |
dc.contributor.author | Kim, Do Wan | - |
dc.contributor.author | Jang, Eun Hyuk | - |
dc.contributor.author | Kwon, Ha Taek | - |
dc.contributor.author | Chi, Young Min | - |
dc.date.accessioned | 2021-09-02T11:25:41Z | - |
dc.date.available | 2021-09-02T11:25:41Z | - |
dc.date.created | 2021-06-19 | - |
dc.date.issued | 2018-05-23 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/75501 | - |
dc.description.abstract | Unsaturated fatty acids are toxic to various bacteria, causing their death or growth inhibition. To prevent this toxicity, unsaturated fatty acids should be converted into saturated fatty acids via hydrogenation reaction, which is the complete reduction of double bonds on the carbon chain. In a recent report, we observed that Stenotrophomonas sp. KCTC 12332 exhibited a high biotransformation activity of oleic acid (OA) in 10-hydroxystearic acid and identified the gene encoding oleate hydratase (OhySt) by complete genomic analysis. In the present study, to further investigate the structural features of OhySt, the recombinant protein was expressed in Escherichia coli, and then purified and crystallized. Biochemical assay showed that OhySt produces 10-hydroxystearic acid in a flavin adenosine dinucleotide (FAD)-dependent manner, indicating that it requires FAD as a cofactor. The OhySt structure, which is determined in its apo state, allows for a structural comparison with the previously reported FAD bound structure of oleate hydratase. The comparison of structures indicates remarkable conformational change of the loop region surrounding the FAD molecule upon binding of FAD. This change forces one of the important catalytic residues into position for catalysis. (C) 2018 Elsevier Inc. All rights reserved. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | - |
dc.subject | DOUBLE-BOND HYDRATASE | - |
dc.subject | FATTY-ACIDS | - |
dc.subject | ANTIBACTERIAL ACTIVITY | - |
dc.subject | OLEIC-ACID | - |
dc.subject | MECHANISM | - |
dc.subject | GROWTH | - |
dc.title | Crystal structure of oleate hydratase from Stenotrophomonas sp KCTC 12332 reveals conformational plasticity surrounding the FAD binding site | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Chi, Young Min | - |
dc.identifier.doi | 10.1016/j.bbrc.2018.03.220 | - |
dc.identifier.scopusid | 2-s2.0-85045570627 | - |
dc.identifier.wosid | 000431286300007 | - |
dc.identifier.bibliographicCitation | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.499, no.4, pp.772 - 776 | - |
dc.relation.isPartOf | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.title | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.volume | 499 | - |
dc.citation.number | 4 | - |
dc.citation.startPage | 772 | - |
dc.citation.endPage | 776 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.subject.keywordPlus | DOUBLE-BOND HYDRATASE | - |
dc.subject.keywordPlus | FATTY-ACIDS | - |
dc.subject.keywordPlus | ANTIBACTERIAL ACTIVITY | - |
dc.subject.keywordPlus | OLEIC-ACID | - |
dc.subject.keywordPlus | MECHANISM | - |
dc.subject.keywordPlus | GROWTH | - |
dc.subject.keywordAuthor | Oleate hydratase | - |
dc.subject.keywordAuthor | Oleic acid | - |
dc.subject.keywordAuthor | 10-Hydroxystearic acid | - |
dc.subject.keywordAuthor | FAD | - |
dc.subject.keywordAuthor | Stenotrophomonas sp KCTC 12332 | - |
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