4XVU

Structure of Get3 bound to the transmembrane domain of Nyv1

Summary for 4XVU

• Entry DOI: 10.2210/pdb4xvu/pdb
• Related: 4XTR 4XWO
• Descriptor: ATPase GET3, Antibody heavy chain, Antibody light chain, ... (8 entities in total)
• Functional Keywords: membrane protein targeting complex, hydrolase-transport protein complex, hydrolase/transport protein
• Biological source: Saccharomyces cerevisiae (ATCC 204508 / S288c) (Baker's yeast); More
• Total number of polymer chains: 14
• Total formula weight: 359087.76

Authors

Mateja, A.,Paduch, M.,Chang, H.-Y.,Szydlowska, A.,Kossiakoff, A.A.,Hegde, R.S.,Keenan, R.J. (deposition date: 2015-01-28, release date: 2015-03-18, Last modification date: 2023-09-27)

Primary citation

Mateja, A.,Paduch, M.,Chang, H.Y.,Szydlowska, A.,Kossiakoff, A.A.,Hegde, R.S.,Keenan, R.J.
Protein targeting. Structure of the Get3 targeting factor in complex with its membrane protein cargo.
Science, 347:1152-1155, 2015

PubMed 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 α-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.

PubMed: 25745174
DOI: 10.1126/science.1261671

Experimental method

X-RAY DIFFRACTION (2.35 Å)