PDBsum entry 4bzk

Protein transport

PDB id: 4bzk

Contents

Protein chains

691 a.a.

279 a.a.

280 a.a.

Waters ×185

PDB id:

4bzk

Name:

Protein transport

Title:

The structure of the copii coat assembled on membranes

Structure:

Protein transport protein sec31. Chain: a, c. Synonym: protein web1. Engineered: yes. Protein transport protein sec13. Chain: b. Engineered: yes. Protein transport protein sec13. Chain: f.

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: sec31, web1, ydl195w, d1229. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932. Gene: sec13, anu3, ylr208w, l8167.4.

Authors:

G.Zanetti,S.Prinz,S.Daum,A.Meister,R.Schekman,K.Bacia,J.A.G.Briggs

Key ref:

G.Zanetti et al. (2013). The structure of the COPII transport-vesicle coat assembled on membranes. Elife, 2, e00951. PubMed id: 24062940 DOI: 10.7554/eLife.00951

Date:

26-Jul-13 Release date: 18-Sep-13

Protein chains

P38968  (SEC31_YEAST) -  Protein transport protein SEC31 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 1273 a.a.

Struc: 691 a.a.*

Protein chain

Q04491  (SEC13_YEAST) -  Protein transport protein SEC13 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 297 a.a.

Struc: 279 a.a.

Protein chain

Q04491  (SEC13_YEAST) -  Protein transport protein SEC13 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 297 a.a.

Struc: 280 a.a.*

* PDB and UniProt seqs differ at 7 residue positions (black crosses)

DOI no: 10.7554/eLife.00951

Elife 2:e00951 (2013)

PubMed id: 24062940

The structure of the COPII transport-vesicle coat assembled on membranes.

G.Zanetti, S.Prinz, S.Daum, A.Meister, R.Schekman, K.Bacia, J.A.Briggs.

ABSTRACT

Coat protein complex II (COPII) mediates formation of the membrane vesicles that export newly synthesised proteins from the endoplasmic reticulum. The inner COPII proteins bind to cargo and membrane, linking them to the outer COPII components that form a cage around the vesicle. Regulated flexibility in coat architecture is essential for transport of a variety of differently sized cargoes, but structural data on the assembled coat has not been available. We have used cryo-electron tomography and subtomogram averaging to determine the structure of the complete, membrane-assembled COPII coat. We describe a novel arrangement of the outer coat and find that the inner coat can assemble into regular lattices. The data reveal how coat subunits interact with one another and with the membrane, suggesting how coordinated assembly of inner and outer coats can mediate and regulate packaging of vesicles ranging from small spheres to large tubular carriers. DOI:http://dx.doi.org/10.7554/eLife.00951.001.