3SJC

Crystal structure of S.cerevisiae Get3 in the semi-open state in complex with Get1 cytosolic domain

Summary for 3SJC

• Entry DOI: 10.2210/pdb3sjc/pdb
• Related: 3SJA 3SJB 3SJD
• Descriptor: ATPase GET3, Golgi to ER traffic protein 1, ZINC ION (3 entities in total)
• Functional Keywords: coiled-coil, receptor complex, ta-protein biogenesis, get pathway, hydrolase-transport protein complex, hydrolase/transport protein
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Cytoplasm: Q12154; Endoplasmic reticulum membrane; Multi-pass membrane protein: P53192
• Total number of polymer chains: 8
• Total formula weight: 193576.79

Authors

Reitz, S.,Wild, K.,Sinning, I. (deposition date: 2011-06-21, release date: 2011-07-06, Last modification date: 2024-02-28)

Primary citation

Stefer, S.,Reitz, S.,Wang, F.,Wild, K.,Pang, Y.Y.,Schwarz, D.,Bomke, J.,Hein, C.,Lohr, F.,Bernhard, F.,Denic, V.,Dotsch, V.,Sinning, I.
Structural basis for tail-anchored membrane protein biogenesis by the Get3-receptor complex.
Science, 333:758-762, 2011

PubMed Abstract: Tail-anchored (TA) proteins are involved in cellular processes including trafficking, degradation, and apoptosis. They contain a C-terminal membrane anchor and are posttranslationally delivered to the endoplasmic reticulum (ER) membrane by the Get3 adenosine triphosphatase interacting with the hetero-oligomeric Get1/2 receptor. We have determined crystal structures of Get3 in complex with the cytosolic domains of Get1 and Get2 in different functional states at 3.0, 3.2, and 4.6 angstrom resolution. The structural data, together with biochemical experiments, show that Get1 and Get2 use adjacent, partially overlapping binding sites and that both can bind simultaneously to Get3. Docking to the Get1/2 complex allows for conformational changes in Get3 that are required for TA protein insertion. These data suggest a molecular mechanism for nucleotide-regulated delivery of TA proteins.

PubMed: 21719644
DOI: 10.1126/science.1207125

Experimental method

X-RAY DIFFRACTION (3.2 Å)