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DC Field | Value | Language |
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dc.citation.endPage | 1901 | - |
dc.citation.number | 12 | - |
dc.citation.startPage | 1673 | - |
dc.citation.title | EMBO REPORTS | - |
dc.citation.volume | 17 | - |
dc.contributor.author | Jeong, Hanbin | - |
dc.contributor.author | Park, Jumi | - |
dc.contributor.author | Lee, Changwook | - |
dc.date.accessioned | 2023-12-21T23:06:43Z | - |
dc.date.available | 2023-12-21T23:06:43Z | - |
dc.date.created | 2016-10-11 | - |
dc.date.issued | 2016-12 | - |
dc.description.abstract | The endoplasmic reticulum-mitochondria encounter structure (ERMES) is a protein complex that plays a tethering role in physically connecting ER and mitochondria membranes. The ERMES complex is composed of Mdm12, Mmm1, and Mdm34, which have a SMP domain in common, and Mdm10. Here, we report the crystal structure of S. cerevisiae Mdm12. The Mdm12 forms a dimeric SMP structure through domain swapping of the β1-strand comprising residues 1-7. Biochemical experiments reveal a phospholipid-binding site located along a hydrophobic channel of the Mdm12 structure and that Mdm12 might have a binding preference for glycerophospholipids harboring a positively charged head group. Strikingly, both full-length Mdm12 and Mdm12 truncated to exclude the disordered region (residues 74-114) display the same organization in the asymmetric unit, although they crystallize as a tetramer and hexamer, respectively. Taken together, these studies provide a novel understanding of the overall organization of SMP domains in the ERMES complex, indicating that Mdm12 interacts with Mdm34 through head-to-head contact, and with Mmm1 through tail-to-tail contact of SMP domains. | - |
dc.identifier.bibliographicCitation | EMBO REPORTS, v.17, no.12, pp.1673 - 1901 | - |
dc.identifier.doi | 10.15252/embr.201642706 | - |
dc.identifier.issn | 1469-221X | - |
dc.identifier.scopusid | 2-s2.0-84999028771 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/20581 | - |
dc.identifier.url | http://embor.embopress.org/content/17/12/1857 | - |
dc.identifier.wosid | 000389329400021 | - |
dc.language | 영어 | - |
dc.publisher | WILEY-BLACKWELL | - |
dc.title | Crystal structure of Mdm12 reveals the architecture and dynamic organization of the ERMES complex | - |
dc.type | Article | - |
dc.description.isOpenAccess | FALSE | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology; Cell Biology | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology; Cell Biology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordAuthor | crystal structure | - |
dc.subject.keywordAuthor | ERMES complex | - |
dc.subject.keywordAuthor | Mdm12 | - |
dc.subject.keywordAuthor | phospholipid binding | - |
dc.subject.keywordAuthor | SMP domain | - |
dc.subject.keywordPlus | ORGANELLE CONTACT SITES | - |
dc.subject.keywordPlus | OUTER-MEMBRANE PROTEIN | - |
dc.subject.keywordPlus | ENDOPLASMIC-RETICULUM | - |
dc.subject.keywordPlus | MTDNA NUCLEOIDS | - |
dc.subject.keywordPlus | SMP DOMAINS | - |
dc.subject.keywordPlus | MITOCHONDRIA | - |
dc.subject.keywordPlus | ER | - |
dc.subject.keywordPlus | YEAST | - |
dc.subject.keywordPlus | PHOSPHOLIPIDS | - |
dc.subject.keywordPlus | MORPHOLOGY | - |
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