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유전체 항상성 연구단
유전체 항상성 연구단
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Crystal structure of Mdm12 reveals the architecture and dynamic organization of the ERMES complex

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Title
Crystal structure of Mdm12 reveals the architecture and dynamic organization of the ERMES complex
Author(s)
Jeong H.; Park J.; Changwook Lee
Publication Date
2016-12
Journal
EMBO REPORTS, v.17, no.12, pp.1857 - 1871
Publisher
NATURE PUBLISHING GROUP
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. © 2016 The Authors
URI
https://pr.ibs.re.kr/handle/8788114/3206
ISSN
1469-221X
Appears in Collections:
Center for Genomic Integrity(유전체 항상성 연구단) > Journal Papers (저널논문)
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