1UGM

Crystal Structure of LC3

1UGM の概要

• エントリーDOI: 10.2210/pdb1ugm/pdb
• 分子名称: Microtubule-associated proteins 1A/1B light chain 3 (2 entities in total)
• 機能のキーワード: lc3, autophagy, structural protein
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Cytoplasm, cytoskeleton: Q62625
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14575.73

構造登録者

Sugawara, K.,Suzuki, N.N.,Fujioka, Y.,Mizushima, N.,Ohsumi, Y.,Inagaki, F. (登録日: 2003-06-16, 公開日: 2004-07-06, 最終更新日: 2023-10-25)

主引用文献

Sugawara, K.,Suzuki, N.N.,Fujioka, Y.,Mizushima, N.,Ohsumi, Y.,Inagaki, F.
The crystal structure of microtubule-associated protein light chain 3, a mammalian homologue of Saccharomyces cerevisiae Atg8
Genes Cells, 9:611-618, 2004

PubMed Abstract: Microtubule-associated protein light chain 3 (LC3), a mammalian homologue of yeast Atg8, plays an essential role in autophagy, which is involved in the bulk degradation of cytoplasmic components by the lysosomal system. Here, we report the crystal structure of LC3 at 2.05 A resolution with an R-factor of 21.8% and a free R-factor of 24.9%. The structure of LC3, which is similar to those of Golgi-associated ATPase enhancer of 16 kDa (GATE-16) and GABAA receptor-associated protein (GABARAP), contains a ubiquitin core with two alpha helices, alpha1 and alpha2, attached at its N-terminus. Some common and distinct features are observed among these proteins, including the conservation of residues required to form an interaction among alpha1, alpha2 and the ubiquitin core. However, the electrostatic potential surfaces of these helices differ, implicating particular roles to select specific binding partners. Hydrophobic patches on the ubiquitin core of LC3, GABARAP and GATE-16 are well conserved and are similar to the E1 binding surface of ubiquitin and NEDD8. Therefore, we propose that the hydrophobic patch is a binding surface for mammalian Atg7 similar to a ubiquitin-like conjugation system. We also propose the functional implications of the ubiquitin fold as a recognition module of target proteins.

PubMed: 15265004
DOI: 10.1111/j.1356-9597.2004.00750.x

実験手法

X-RAY DIFFRACTION (2.05 Å)