4XTR: Structure of Get3 bound to the transmembrane domain of Pep12

Citation:
Abstract
Tail-anchored (TA) proteins are a physiologically important class of membrane proteins targeted to the endoplasmic reticulum by the conserved guided-entry of TA proteins (GET) pathway. During transit, their hydrophobic transmembrane domains (TMDs) are chaperoned by the cytosolic targeting factor Get3, but the molecular nature of the functional Get3-TA protein targeting complex remains unknown. We reconstituted the physiologic assembly pathway for a functional targeting complex and showed that it comprises a TA protein bound to a Get3 homodimer. Crystal structures of Get3 bound to different TA proteins showed an alpha-helical TMD occupying a hydrophobic groove that spans the Get3 homodimer. Our data elucidate the mechanism of TA protein recognition and shielding by Get3 and suggest general principles of hydrophobic domain chaperoning by cellular targeting factors.
PDB ID: 4XTRDownload
MMDB ID: 127953
PDB Deposition Date: 2015/1/23
Updated in MMDB: 2017/10
Experimental Method:
x-ray diffraction
Resolution: 2.05  Å
Source Organism:
Saccharomyces cerevisiae Vin13
Similar Structures:
Biological Unit for 4XTR: heptameric; determined by author and by software (PISA)
Molecular Components in 4XTR
Label Count Molecule
Proteins (7 molecules)
2
Atpase Get3(Gene symbol: GET3)
Molecule annotation
2
Antibody Heavy Chain
Molecule annotation
2
Antibody Light Chain
Molecule annotation
1
Pep12p
Molecule annotation
Chemicals (7 molecules)
1
2
2
2
3
1
4
2
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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