4TQ0: Crystal Structure Of Human Atg5-atg16n69

Autophagy is a bulky catabolic process that responds to nutrient homeostasis and extracellular stress signals and is a conserved mechanism in all eukaryotes. When autophagy is induced, cellular components are sequestered within an autophagosome and finally degraded by subsequent fusion with a lysosome. During this process, the ATG12-ATG5 conjugate requires 2 different binding partners, ATG16L1 for autophagosome elongation and TECPR1 for lysosomal fusion. In our current study, we describe the crystal structures of human ATG5 in complex with an N-terminal domain of ATG16L1 as well as an internal AIR domain of TECPR1. Both binding partners exhibit a similar alpha-helical structure containing a conserved binding motif termed AFIM. Furthermore, we characterize the critical role of the C-terminal unstructured region of the AIR domain of TECPR1. These findings are further confirmed by biochemical and cell biological analyses. These results provide new insights into the molecular details of the autophagosome maturation process, from its elongation to its fusion with a lysosome.
PDB ID: 4TQ0Download
MMDB ID: 127699
PDB Deposition Date: 2014/6/10
Updated in MMDB: 2015/03
Experimental Method:
x-ray diffraction
Resolution: 2.7  Å
Source Organism:
Similar Structures:
Biological Unit for 4TQ0: dimeric; determined by author and by software (PISA)
Molecular Components in 4TQ0
Label Count Molecule
Proteins (2 molecules)
Autophagy Protein 5(Gene symbol: ATG5)
Molecule annotation
Autophagy-related Protein 16-1(Gene symbol: ATG16L1)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB