Full metadata record
DC Field | Value | Language |
---|---|---|
dc.citation.startPage | 382 | - |
dc.citation.title | NATURE COMMUNICATIONS | - |
dc.citation.volume | 9 | - |
dc.contributor.author | Joo, Seongjoon | - |
dc.contributor.author | Cho, In Jin | - |
dc.contributor.author | Seo, Hogyun | - |
dc.contributor.author | Son, Hyeoncheol Francis | - |
dc.contributor.author | Sagong, Hye-Young | - |
dc.contributor.author | Shin, Tae Joo | - |
dc.contributor.author | Choi, So Young | - |
dc.contributor.author | Lee, Sang Yup | - |
dc.contributor.author | Kim, Kyung-Jin | - |
dc.date.accessioned | 2023-12-21T21:14:02Z | - |
dc.date.available | 2023-12-21T21:14:02Z | - |
dc.date.created | 2018-02-08 | - |
dc.date.issued | 2018-01 | - |
dc.description.abstract | Plastics, including poly(ethylene terephthalate) (PET), possess many desirable characteristics and thus are widely used in daily life. However, non-biodegradability, once thought to be an advantage offered by plastics, is causing major environmental problem. Recently, a PET-degrading bacterium, Ideonella sakaiensis, was identified and suggested for possible use in degradation and/or recycling of PET. However, the molecular mechanism of PET degradation is not known. Here we report the crystal structure of I. sakaiensis PETase (IsPETase) at 1.5 angstrom resolution. IsPETase has a Ser-His-Asp catalytic triad at its active site and contains an optimal substrate binding site to accommodate four monohydroxyethyl terephthalate (MHET) moieties of PET. Based on structural and site-directed mutagenesis experiments, the detailed process of PET degradation into MHET, terephthalic acid, and ethylene glycol is suggested. Moreover, other PETase candidates potentially having high PET-degrading activities are suggested based on phylogenetic tree analysis of 69 PETase-like proteins. | - |
dc.identifier.bibliographicCitation | NATURE COMMUNICATIONS, v.9, pp.382 | - |
dc.identifier.doi | 10.1038/s41467-018-02881-1 | - |
dc.identifier.issn | 2041-1723 | - |
dc.identifier.scopusid | 2-s2.0-85041215448 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/23658 | - |
dc.identifier.url | https://www.nature.com/articles/s41467-018-02881-1 | - |
dc.identifier.wosid | 000423430900002 | - |
dc.language | 영어 | - |
dc.publisher | NATURE PUBLISHING GROUP | - |
dc.title | Structural insight into molecular mechanism of poly (ethylene terephthalate) degradation | - |
dc.type | Article | - |
dc.description.isOpenAccess | TRUE | - |
dc.relation.journalWebOfScienceCategory | Multidisciplinary Sciences | - |
dc.relation.journalResearchArea | Science & Technology - Other Topics | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordPlus | ALPHA/BETA-HYDROLASE FOLD | - |
dc.subject.keywordPlus | POLYETHYLENE TEREPHTHALATE | - |
dc.subject.keywordPlus | THERMOBIFIDA-FUSCA | - |
dc.subject.keywordPlus | CUTINASE | - |
dc.subject.keywordPlus | HYDROLYSIS | - |
dc.subject.keywordPlus | POLY(ETHYLENE-TEREPHTHALATE) | - |
dc.subject.keywordPlus | REPLACEMENT | - |
dc.subject.keywordPlus | SEQUENCE | - |
dc.subject.keywordPlus | DOCKING | - |
dc.subject.keywordPlus | SYSTEM | - |
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