3WO7

Crystal structure of YidC from Bacillus halodurans (form II)

3WO7 の概要

• エントリーDOI: 10.2210/pdb3wo7/pdb
• 関連するPDBエントリー: 3w06
• 分子名称: Membrane protein insertase YidC 2, COPPER (II) ION (2 entities in total)
• 機能のキーワード: alpha helical, membrane protein
• 由来する生物種: Bacillus halodurans
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 58837.55

構造登録者

Kumazaki, K.,Tsukazaki, T.,Ishitani, R.,Nureki, O. (登録日: 2013-12-20, 公開日: 2014-04-23, 最終更新日: 2024-04-03)

主引用文献

Kumazaki, K.,Chiba, S.,Takemoto, M.,Furukawa, A.,Nishiyama, K.,Sugano, Y.,Mori, T.,Dohmae, N.,Hirata, K.,Nakada-Nakura, Y.,Maturana, A.D.,Tanaka, Y.,Mori, H.,Sugita, Y.,Arisaka, F.,Ito, K.,Ishitani, R.,Tsukazaki, T.,Nureki, O.
Structural basis of Sec-independent membrane protein insertion by YidC.
Nature, 509:516-520, 2014

PubMed Abstract: Newly synthesized membrane proteins must be accurately inserted into the membrane, folded and assembled for proper functioning. The protein YidC inserts its substrates into the membrane, thereby facilitating membrane protein assembly in bacteria; the homologous proteins Oxa1 and Alb3 have the same function in mitochondria and chloroplasts, respectively. In the bacterial cytoplasmic membrane, YidC functions as an independent insertase and a membrane chaperone in cooperation with the translocon SecYEG. Here we present the crystal structure of YidC from Bacillus halodurans, at 2.4 Å resolution. The structure reveals a novel fold, in which five conserved transmembrane helices form a positively charged hydrophilic groove that is open towards both the lipid bilayer and the cytoplasm but closed on the extracellular side. Structure-based in vivo analyses reveal that a conserved arginine residue in the groove is important for the insertion of membrane proteins by YidC. We propose an insertion mechanism for single-spanning membrane proteins, in which the hydrophilic environment generated by the groove recruits the extracellular regions of substrates into the low-dielectric environment of the membrane.

PubMed: 24739968
DOI: 10.1038/nature13167

実験手法

X-RAY DIFFRACTION (3.201 Å)