3IBG

Crystal structure of Aspergillus fumigatus Get3 with bound ADP

Summary for 3IBG

• Entry DOI: 10.2210/pdb3ibg/pdb
• Descriptor: ATPase, subunit of the Get complex, ADENOSINE-5'-DIPHOSPHATE (2 entities in total)
• Functional Keywords: nucleotide binding, hydrolase, deviant walker a motif
• Biological source: Aspergillus fumigatus (Sartorya fumigata)
• Cellular location: Cytoplasm (By similarity): Q4WY07
• Total number of polymer chains: 6
• Total formula weight: 233665.30

Authors

Suloway, C.J.M.,Chartron, J.W.,Zaslaver, M.,Clemons Jr., W.M. (deposition date: 2009-07-15, release date: 2009-08-25, Last modification date: 2024-11-20)

Primary citation

Suloway, C.J.,Chartron, J.W.,Zaslaver, M.,Clemons, W.M.
Model for eukaryotic tail-anchored protein binding based on the structure of Get3
Proc.Natl.Acad.Sci.USA, 106:14849-14854, 2009

PubMed Abstract: The Get3 ATPase directs the delivery of tail-anchored (TA) proteins to the endoplasmic reticulum (ER). TA-proteins are characterized by having a single transmembrane helix (TM) at their extreme C terminus and include many essential proteins, such as SNAREs, apoptosis factors, and protein translocation components. These proteins cannot follow the SRP-dependent co-translational pathway that typifies most integral membrane proteins; instead, post-translationally, these proteins are recognized and bound by Get3 then delivered to the ER in the ATP dependent Get pathway. To elucidate a molecular mechanism for TA protein binding by Get3 we have determined three crystal structures in apo and ADP forms from Saccharomyces cerevisae (ScGet3-apo) and Aspergillus fumigatus (AfGet3-apo and AfGet3-ADP). Using structural information, we generated mutants to confirm important interfaces and essential residues. These results point to a model of how Get3 couples ATP hydrolysis to the binding and release of TA-proteins.

PubMed: 19706470
DOI: 10.1073/pnas.0907522106

Experimental method

X-RAY DIFFRACTION (3.2 Å)