4TQ1

Crystal structure of human ATG5-TECAIR

Summary for 4TQ1

• Entry DOI: 10.2210/pdb4tq1/pdb
• Related: 4TQ0
• Descriptor: Autophagy protein 5, Tectonin beta-propeller repeat-containing protein 1 (3 entities in total)
• Functional Keywords: autophagy protein complex, protein binding
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 2
• Total formula weight: 38884.26

Authors

Kim, J.H.,Hong, S.B.,Song, H.K. (deposition date: 2014-06-10, release date: 2015-03-11, Last modification date: 2024-03-20)

Primary citation

Kim, J.H.,Hong, S.B.,Lee, J.K.,Han, S.,Roh, K.H.,Lee, K.E.,Kim, Y.K.,Choi, E.J.,Song, H.K.
Insights into autophagosome maturation revealed by the structures of ATG5 with its interacting partners
Autophagy, 11:75-87, 2015

PubMed Abstract: 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 α-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.

PubMed: 25484072
DOI: 10.4161/15548627.2014.984276

Experimental method

X-RAY DIFFRACTION (1.802 Å)