7LK3

Crystal structure of untwinned human GABARAPL2

7LK3 の概要

• エントリーDOI: 10.2210/pdb7lk3/pdb
• 分子名称: Gamma-aminobutyric acid receptor-associated protein-like 2, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: autophagy, autophagosome, atg8 family, ubiquitin-like, signaling protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28128.54

構造登録者

Scicluna, K.,Dewson, G.,Czabotar, P.E.,Birkinshaw, R.W. (登録日: 2021-02-01, 公開日: 2021-05-12, 最終更新日: 2023-10-18)

主引用文献

Scicluna, K.,Dewson, G.,Czabotar, P.E.,Birkinshaw, R.W.
A new crystal form of GABARAPL2.
Acta Crystallogr.,Sect.F, 77:140-147, 2021

PubMed Abstract: The Atg8 protein family comprises the GABA type A receptor-associated proteins (GABARAPs) and microtubule-associated protein 1 light chains 3 (MAP1LC3s) that are essential mediators of autophagy. The LC3-interacting region (LIR) motifs of autophagy receptors and adaptors bind Atg8 proteins to promote autophagosome formation, cargo recruitment, and autophagosome closure and fusion to lysosomes. A crystal structure of human GABARAPL2 has been published [PDB entry 4co7; Ma et al. (2015), Biochemistry, 54, 5469-5479]. This was crystallized in space group P2 with a monoclinic angle of 90° and shows a pseudomerohedral twinning pathology. This article reports a new, untwinned GABARAPL2 crystal form, also in space group P2, but with a 98° monoclinic angle. No major conformational differences were observed between the structures. In the structure described here, the C-terminal Phe117 binds into the LIR docking site (LDS) of a neighbouring molecule within the asymmetric unit, as observed in the previously reported structure. This crystal contact blocks the LDS for co-crystallization with ligands. Phe117 of GABARAPL2 is normally removed during biological processing by Atg4 family proteases. These data indicate that to establish interactions with the LIR, Phe117 should be removed to eliminate the crystal contact and liberate the LDS for co-crystallization with LIR peptides.

PubMed: 33949974
DOI: 10.1107/S2053230X21004489

実験手法

X-RAY DIFFRACTION (1.9 Å)