Structural and Biochemical Study of the Mono-ADP-Ribosyltransferase Domain of SdeA, a Ubiquitylating/Deubiquitylating Enzyme from Legionella pneumophila
DC Field | Value | Language |
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dc.contributor.author | Kim, Leehyeon | - |
dc.contributor.author | Kwon, Do Hoon | - |
dc.contributor.author | Kim, Bong Heon | - |
dc.contributor.author | Kim, Jiyeon | - |
dc.contributor.author | Park, Mi Rae | - |
dc.contributor.author | Park, Zee-Yong | - |
dc.contributor.author | Song, Hyun Kyu | - |
dc.date.accessioned | 2021-09-02T07:39:39Z | - |
dc.date.available | 2021-09-02T07:39:39Z | - |
dc.date.created | 2021-06-16 | - |
dc.date.issued | 2018-08-17 | - |
dc.identifier.issn | 0022-2836 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/73753 | - |
dc.description.abstract | Conventional ubiquitylation occurs through an ATP-dependent three-enzyme cascade (E1, E2, and E3) that mediates the covalent conjugation of the C-terminus of ubiquitin to a lysine on the substrate. SdeA, which belongs to the SidE effector family of Legionella pneumophila, can transfer ubiquitin to endoplasmic reticulum-associated Rab-family GTPases in a manner independent of El and E2 enzymes. The novel ubiquitin-modifying enzyme SdeA utilizes NAD(+) as a cofactor to attach ubiquitin to a serine residue of the substrate. Here, to elucidate the coupled enzymatic reaction of NAD+ hydrolysis and ADP-ribosylation of ubiquitin in SdeA, we characterized the mono-ADP-ribosyltransferase domain of SdeA and show that it consists of two sub-domains termed mART-N and mART-C. The crystal structure of the mART-C domain of SdeA was also determined in free form and in complex with NAD(+) at high resolution. Furthermore, the spatial orientations of the N-terminal deubiquitylase, phosphodiesterase, mono-ADP-ribosyltransferase, and C-terminal coiled-coil domains within the 180-kDa full-length SdeA were determined. These results provide insight into the unusual ubiquitylation mechanism of SdeA and expand our knowledge on the structure-function of mono-ADP-ribosyltransferases. (C) 2018 Elsevier Ltd. All rights reserved. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD | - |
dc.subject | CLOSTRIDIUM-BOTULINUM | - |
dc.subject | SUBSTRATE RECOGNITION | - |
dc.subject | UBIQUITIN SYSTEM | - |
dc.subject | CATALYTIC SITE | - |
dc.subject | TOXIN | - |
dc.subject | MECHANISM | - |
dc.subject | EFFECTOR | - |
dc.subject | BACTERIA | - |
dc.subject | MOTIF | - |
dc.subject | HOST | - |
dc.title | Structural and Biochemical Study of the Mono-ADP-Ribosyltransferase Domain of SdeA, a Ubiquitylating/Deubiquitylating Enzyme from Legionella pneumophila | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Song, Hyun Kyu | - |
dc.identifier.doi | 10.1016/j.jmb.2018.05.043 | - |
dc.identifier.scopusid | 2-s2.0-85048471538 | - |
dc.identifier.wosid | 000441645300020 | - |
dc.identifier.bibliographicCitation | JOURNAL OF MOLECULAR BIOLOGY, v.430, no.17, pp.2843 - 2856 | - |
dc.relation.isPartOf | JOURNAL OF MOLECULAR BIOLOGY | - |
dc.citation.title | JOURNAL OF MOLECULAR BIOLOGY | - |
dc.citation.volume | 430 | - |
dc.citation.number | 17 | - |
dc.citation.startPage | 2843 | - |
dc.citation.endPage | 2856 | - |
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.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.subject.keywordPlus | CLOSTRIDIUM-BOTULINUM | - |
dc.subject.keywordPlus | SUBSTRATE RECOGNITION | - |
dc.subject.keywordPlus | UBIQUITIN SYSTEM | - |
dc.subject.keywordPlus | CATALYTIC SITE | - |
dc.subject.keywordPlus | TOXIN | - |
dc.subject.keywordPlus | MECHANISM | - |
dc.subject.keywordPlus | EFFECTOR | - |
dc.subject.keywordPlus | BACTERIA | - |
dc.subject.keywordPlus | MOTIF | - |
dc.subject.keywordPlus | HOST | - |
dc.subject.keywordAuthor | Legionella pneumophila | - |
dc.subject.keywordAuthor | mART | - |
dc.subject.keywordAuthor | NAD(+) | - |
dc.subject.keywordAuthor | SdeA | - |
dc.subject.keywordAuthor | ubiquitin | - |
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