4J2G

Atg13 HORMA domain

4J2G の概要

• エントリーDOI: 10.2210/pdb4j2g/pdb
• 分子名称: KLTH0A00704p, SULFATE ION (3 entities in total)
• 機能のキーワード: autophagy, horma, atg13, unknown function
• 由来する生物種: Lachancea thermotolerans (Yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 61206.20

構造登録者

Jao, C.,Stanley, R.E.,Ragusa, M.J.,Hurley, J.H. (登録日: 2013-02-04, 公開日: 2013-03-20, 最終更新日: 2024-11-20)

主引用文献

Jao, C.C.,Ragusa, M.J.,Stanley, R.E.,Hurley, J.H.
A HORMA domain in Atg13 mediates PI 3-kinase recruitment in autophagy.
Proc.Natl.Acad.Sci.USA, 110:5486-5491, 2013

PubMed Abstract: Autophagy-related 13 (Atg13) is a key early-acting factor in autophagy and the major locus for nutrient-dependent regulation of autophagy by Tor. The 2.3-Å resolution crystal structure of the N-terminal domain of Atg13 reveals a previously unidentified HORMA (Hop1p, Rev1p and Mad2) domain similar to that of the spindle checkpoint protein Mad2. Mad2 has two different stable conformations, O-Mad2 and C-Mad2, and the Atg13 HORMA structure corresponds to the C-Mad2 state. The Atg13 HORMA domain is required for autophagy and for recruitment of the phosphatidylinositol (PI) 3-kinase subunit Atg14 but is not required for Atg1 interaction or Atg13 recruitment to the preautophagosomal structure. The Atg13 HORMA structure reveals a pair of conserved Arg residues that constitute a putative phosphate sensor. One of the Arg residues is in the region corresponding to the "safety belt" conformational switch of Mad2, suggesting conformational regulation of phosphate binding. These two Arg residues are essential for autophagy, suggesting that the Atg13 HORMA domain could function as a phosphoregulated conformational switch.

PubMed: 23509291
DOI: 10.1073/pnas.1220306110

実験手法

X-RAY DIFFRACTION (2.29 Å)