PDBsum entry 4tq1

Protein binding

PDB id: 4tq1

Contents

Protein chains

258 a.a.

32 a.a.

Waters ×190

PDB id:

4tq1

Name:

Protein binding

Title:

Crystal structure of human atg5-tecair

Structure:

Autophagy protein 5. Chain: a. Synonym: apg5-like,apoptosis-specific protein. Engineered: yes. Tectonin beta-propeller repeat-containing protein 1. Chain: b. Fragment: unp residues 503-540. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: atg5, apg5l, asp. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Gene: tecpr1, kiaa1358. Expression_system_taxid: 469008

Resolution:

1.80Å R-factor: 0.181 R-free: 0.222

Authors:

J.H.Kim,S.B.Hong,H.K.Song

Key ref:

J.H.Kim et al. (2015). Insights into autophagosome maturation revealed by the structures of ATG5 with its interacting partners. Autophagy, 11, 75-87. PubMed id: 25484072 DOI: 10.4161/15548627.2014.984276

Date:

10-Jun-14 Release date: 11-Mar-15

Protein chain

Q9H1Y0  (ATG5_HUMAN) -  Autophagy protein 5 from Homo sapiens

Seq: 275 a.a.

Struc: 258 a.a.

Protein chain

Q7Z6L1  (TCPR1_HUMAN) -  Tectonin beta-propeller repeat-containing protein 1 from Homo sapiens

Seq: 1165 a.a.

Struc: 32 a.a.

DOI no: 10.4161/15548627.2014.984276

Autophagy 11:75-87 (2015)

PubMed id: 25484072

Insights into autophagosome maturation revealed by the structures of ATG5 with its interacting partners.

J.H.Kim, S.B.Hong, J.K.Lee, S.Han, K.H.Roh, K.E.Lee, Y.K.Kim, E.J.Choi, H.K.Song.

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.