3ZS9

S. cerevisiae Get3-ADP-AlF4- complex with a cytosolic Get2 fragment

Summary for 3ZS9

• Entry DOI: 10.2210/pdb3zs9/pdb
• Related: 2WOJ 3ZS8
• Descriptor: ATPASE GET3, GOLGI TO ER TRAFFIC PROTEIN 2, ADENOSINE-5'-DIPHOSPHATE, ... (7 entities in total)
• Functional Keywords: hydrolase-transport protein complex, membrane protein, targeting factor, hydrolase/transport protein
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Cellular location: Cytoplasm: Q12154; Endoplasmic reticulum membrane; Multi-pass membrane protein: P40056
• Total number of polymer chains: 4
• Total formula weight: 88651.47

Authors

Mariappan, M.,Mateja, A.,Dobosz, M.,Bove, E.,Hegde, R.S.,Keenan, R.J. (deposition date: 2011-06-24, release date: 2011-09-07, Last modification date: 2023-12-20)

Primary citation

Mariappan, M.,Mateja, A.,Dobosz, M.,Bove, E.,Hegde, R.S.,Keenan, R.J.
The Mechanism of Membrane-Associated Steps in Tail-Anchored Protein Insertion.
Nature, 477:61-, 2011

PubMed Abstract: Tail-anchored (TA) membrane proteins destined for the endoplasmic reticulum are chaperoned by cytosolic targeting factors that deliver them to a membrane receptor for insertion. Although a basic framework for TA protein recognition is now emerging, the decisive targeting and membrane insertion steps are not understood. Here we reconstitute the TA protein insertion cycle with purified components, present crystal structures of key complexes between these components and perform mutational analyses based on the structures. We show that a committed targeting complex, formed by a TA protein bound to the chaperone ATPase Get3, is initially recruited to the membrane through an interaction with Get2. Once the targeting complex has been recruited, Get1 interacts with Get3 to drive TA protein release in an ATPase-dependent reaction. After releasing its TA protein cargo, the now-vacant Get3 recycles back to the cytosol concomitant with ATP binding. This work provides a detailed structural and mechanistic framework for the minimal TA protein insertion cycle.

PubMed: 21866104
DOI: 10.1038/NATURE10362

Experimental method

X-RAY DIFFRACTION (2.095 Å)