5XDN

Crystal structure of human voltage-dependent anion channel 1 (hVDAC1) in P22121 space group

5XDN の概要

• エントリーDOI: 10.2210/pdb5xdn/pdb
• 関連するPDBエントリー: 5XDO
• 分子名称: Voltage-dependent anion-selective channel protein 1, DODECANE, HEXANE, ... (6 entities in total)
• 機能のキーワード: membrane protein, beta-barrel structure, cell-free synthesis
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Mitochondrion outer membrane ; Multi-pass membrane protein : P21796
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 65510.24

構造登録者

Hosaka, T.,Kimura-Someya, T.,Shirouzu, M. (登録日: 2017-03-28, 公開日: 2017-06-28, 最終更新日: 2023-11-22)

主引用文献

Hosaka, T.,Okazaki, M.,Kimura-Someya, T.,Ishizuka-Katsura, Y.,Ito, K.,Yokoyama, S.,Dodo, K.,Sodeoka, M.,Shirouzu, M.
Crystal structural characterization reveals novel oligomeric interactions of human voltage-dependent anion channel 1
Protein Sci., 26:1749-1758, 2017

PubMed Abstract: Voltage-dependent anion channel 1 (VDAC1), which is located in the outer mitochondrial membrane, plays important roles in various cellular processes. For example, oligomerization of VDAC1 is involved in the release of cytochrome c to the cytoplasm, leading to apoptosis. However, it is unknown how VDAC1 oligomerization occurs in the membrane. In the present study, we determined high-resolution crystal structures of oligomeric human VDAC1 (hVDAC1) prepared by using an Escherichia coli cell-free protein synthesis system, which avoided the need for denaturation and refolding of the protein. Broad-range screening using a bicelle crystallization method produced crystals in space groups C222 and P22 2 , which diffracted to a resolution of 3.10 and 3.15 Å, respectively. Each crystal contained two hVDAC1 protomers in the asymmetric unit. Dimer within the asymmetrical unit of the crystal in space group C222 were oriented parallel, whereas those of the crystal in space group P22 2 were oriented anti-parallel. From a model of the crystal in space group C222, which we constructed by using crystal symmetry operators, a heptameric structure with eight patterns of interaction between protomers, including hydrophobic interactions with β-strands, hydrophilic interactions with loop regions, and protein-lipid interactions, was observed. It is possible that by having multiple patterns of interaction, VDAC1 can form homo- or hetero-oligomers not only with other VDAC1 protomers but also with other proteins such as VDAC2, VDAC3 and apoptosis-regulating proteins in the Bcl-2 family.

PubMed: 28608415
DOI: 10.1002/pro.3211

実験手法

X-RAY DIFFRACTION (3.15 Å)