5H5C

Mdm12 from K. lactis (1-239), uniformly Lys dimethyl modified, crystallized in FOS-MEA-10

5H5C の概要

• エントリーDOI: 10.2210/pdb5h5c/pdb
• 関連するPDBエントリー: 5H54 5H55 5H5A
• 分子名称: Mitochondrial distribution and morphology protein 12 (1 entity in total)
• 機能のキーワード: lipid binding protein
• 由来する生物種: Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast)
• 細胞内の位置: Mitochondrion outer membrane ; Peripheral membrane protein ; Cytoplasmic side : Q6CUC3
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27466.43

構造登録者

Kawano, S.,Quinbara, S.,Endo, T. (登録日: 2016-11-05, 公開日: 2017-11-08, 最終更新日: 2024-03-20)

主引用文献

Kawano, S.,Tamura, Y.,Kojima, R.,Bala, S.,Asai, E.,Michel, A.H.,Kornmann, B.,Riezman, I.,Riezman, H.,Sakae, Y.,Okamoto, Y.,Endo, T.
Structure-function insights into direct lipid transfer between membranes by Mmm1-Mdm12 of ERMES
J. Cell Biol., 217:959-974, 2018

PubMed Abstract: The endoplasmic reticulum (ER)-mitochondrial encounter structure (ERMES) physically links the membranes of the ER and mitochondria in yeast. Although the ER and mitochondria cooperate to synthesize glycerophospholipids, whether ERMES directly facilitates the lipid exchange between the two organelles remains controversial. Here, we compared the x-ray structures of an ERMES subunit Mdm12 from with that of Mdm12 from and found that both Mdm12 proteins possess a hydrophobic pocket for phospholipid binding. However in vitro lipid transfer assays showed that Mdm12 alone or an Mmm1 (another ERMES subunit) fusion protein exhibited only a weak lipid transfer activity between liposomes. In contrast, Mdm12 in a complex with Mmm1 mediated efficient lipid transfer between liposomes. Mutations in Mmm1 or Mdm12 impaired the lipid transfer activities of the Mdm12-Mmm1 complex and furthermore caused defective phosphatidylserine transport from the ER to mitochondrial membranes via ERMES in vitro. Therefore, the Mmm1-Mdm12 complex functions as a minimal unit that mediates lipid transfer between membranes.

PubMed: 29279306
DOI: 10.1083/jcb.201704119

実験手法

X-RAY DIFFRACTION (3.31 Å)