PDBsum entry 4hpq

Protein transport

PDB id: 4hpq

Contents

Protein chains

69 a.a.

115 a.a.

396 a.a.

PDB id:

4hpq

Name:

Protein transport

Title:

Crystal structure of the atg17-atg31-atg29 complex

Structure:

Atg29. Chain: a, d. Synonym: klth0c07942p. Engineered: yes. Atg31. Chain: b, e. Synonym: klth0d11660p. Engineered: yes. Mutation: yes.

Source:

Lachancea thermotolerans cbs 6340. Yeast. Organism_taxid: 559295. Strain: atcc 56472 / cbs 6340 / nrrl y-8284. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

3.06Å R-factor: 0.305 R-free: 0.336

Authors:

R.E.Stanley,M.J.Ragusa,J.H.Hurley

Key ref:

M.J.Ragusa et al. (2012). Architecture of the Atg17 complex as a scaffold for autophagosome biogenesis. Cell, 151, 1501-1512. PubMed id: 23219485

Date:

24-Oct-12 Release date: 26-Dec-12

Protein chains

C5DF24  (C5DF24_LACTC) -  Autophagy-related protein 29 from Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)

Seq: 171 a.a.

Struc: 69 a.a.*

Protein chains

C5DEB9  (C5DEB9_LACTC) -  KLTH0C07942p from Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)

Seq: 145 a.a.

Struc: 115 a.a.*

Protein chains

C5DFJ6  (C5DFJ6_LACTC) -  Autophagy-related protein 17 from Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)

Seq: 413 a.a.

Struc: 396 a.a.

* PDB and UniProt seqs differ at 31 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chains A, B, C, D, E, F: E.C.?

Cell 151:1501-1512 (2012)

PubMed id: 23219485

Architecture of the Atg17 complex as a scaffold for autophagosome biogenesis.

M.J.Ragusa, R.E.Stanley, J.H.Hurley.

ABSTRACT

Macroautophagy is a bulk clearance mechanism in which the double-membraned phagophore grows and engulfs cytosolic material. In yeast, the phagophore nucleates from a cluster of 20-30 nm diameter Atg9-containing vesicles located at a multiprotein assembly known as the preautophagosomal structure (PAS). The crystal structure of a 2:2:2 complex of the earliest acting PAS proteins, Atg17, Atg29, and Atg31, was solved at 3.05 Å resolution. Atg17 is crescent shaped with a 10 nm radius of curvature. Dimerization of the Atg17-Atg31-Atg29 complex is critical for both PAS formation and autophagy, and each dimer contains two separate and complete crescents. Upon induction of autophagy, Atg17-Atg31-Atg29 assembles with Atg1 and Atg13, which in turn initiates the formation of the phagophore. The C-terminal EAT domain of Atg1 was shown to sense membrane curvature, dimerize, and tether lipid vesicles. These data suggest a structural mechanism for the organization of Atg9 vesicles into the early phagophore.