4PWX

Crystal structure of an ATP-bound Get3-Get4-Get5 complex from S.cerevisiae

Summary for 4PWX

• Entry DOI: 10.2210/pdb4pwx/pdb
• Descriptor: ATPase GET3, Golgi to ER traffic protein 4, Ubiquitin-like protein MDY2, ... (6 entities in total)
• Functional Keywords: tail-anchored targeting, transport protein
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Cytoplasm: Q12154 Q12125; Cytoplasm, cytosol: Q12285
• Total number of polymer chains: 6
• Total formula weight: 159904.21

Authors

Gristick, H.B.,Clemons Jr., W.M. (deposition date: 2014-03-21, release date: 2014-04-09, Last modification date: 2023-09-20)

Primary citation

Gristick, H.B.,Rao, M.,Chartron, J.W.,Rome, M.E.,Shan, S.O.,Clemons, W.M.
Crystal structure of ATP-bound Get3-Get4-Get5 complex reveals regulation of Get3 by Get4.
Nat.Struct.Mol.Biol., 21:437-442, 2014

PubMed Abstract: Correct localization of membrane proteins is essential to all cells. Chaperone cascades coordinate the capture and handover of substrate proteins from the ribosomes to the target membranes, yet the mechanistic and structural details of these processes remain unclear. Here we investigate the conserved GET pathway, in which the Get4-Get5 complex mediates the handover of tail-anchor (TA) substrates from the cochaperone Sgt2 to the Get3 ATPase, the central targeting factor. We present a crystal structure of a yeast Get3-Get4-Get5 complex in an ATP-bound state and show how Get4 primes Get3 by promoting the optimal configuration for substrate capture. Structure-guided biochemical analyses demonstrate that Get4-mediated regulation of ATP hydrolysis by Get3 is essential to efficient TA-protein targeting. Analogous regulation of other chaperones or targeting factors could provide a general mechanism for ensuring effective substrate capture during protein biogenesis.

PubMed: 24727835
DOI: 10.1038/nsmb.2813

Experimental method

X-RAY DIFFRACTION (5.4 Å)