4BM5

Chloroplast inner membrane protein TIC110

4BM5 の概要

• エントリーDOI: 10.2210/pdb4bm5/pdb
• 分子名称: SIMILAR TO CHLOROPLAST INNER MEMBRANE PROTEIN TIC110 (1 entity in total)
• 機能のキーワード: protein transport
• 由来する生物種: CYANIDIOSCHYZON MEROLAE
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39470.63

構造登録者

Tsai, J.-Y.,Chu, C.-C.,Yeh, Y.-H.,Chen, L.-J.,Li, H.-m.,Hsiao, C.-D. (登録日: 2013-05-06, 公開日: 2013-06-12, 最終更新日: 2024-05-08)

主引用文献

Tsai, J.-Y.,Chu, C.-C.,Yeh, Y.-H.,Chen, L.-J.,Li, H.-M.,Hsiao, C.-D.
Structural Characterizations of Chloroplast Translocon Protein Tic110.
Plant J., 75:847-, 2013

PubMed Abstract: Tic110 is a major component of the chloroplast protein import translocon. Two functions with mutually exclusive structures have been proposed for Tic110: a protein-conducting channel with six transmembrane domains and a scaffold with two N-terminal transmembrane domains followed by a large soluble domain for binding transit peptides and other stromal translocon components. To investigate the structure of Tic110, Tic110 from Cyanidioschyzon merolae (CmTic110) was characterized. We constructed three fragments, CmTic110A , CmTic110B and CmTic110C , with increasing N-terminal truncations, to perform small-angle X-ray scattering (SAXS) and X-ray crystallography analyses and Dali structural comparison. Here we report the molecular envelope of CmTic110B and CmTic110C determined by SAXS, and the crystal structure of CmTic110C at 4.2 Å. Our data indicate that the C-terminal half of CmTic110 possesses a rod-shaped helix-repeat structure that is too flattened and elongated to be a channel. The structure is most similar to the HEAT-repeat motif that functions as scaffolds for protein-protein interactions.

PubMed: 23711301
DOI: 10.1111/TPJ.12249

実験手法

X-RAY DIFFRACTION (4.2 Å)