3A37

Structural insight into the membrane insertion of tail-anchored proteins by Get3

Summary for 3A37

• Entry DOI: 10.2210/pdb3a37/pdb
• Related: 3A36
• Descriptor: ATPase GET3, ADENOSINE-5'-DIPHOSPHATE, ZINC ION (3 entities in total)
• Functional Keywords: homo dimer, atpase, zinc binding, arsenical resistance, atp-binding, cytoplasm, endoplasmic reticulum, er-golgi transport, golgi apparatus, hydrolase, nucleotide-binding, transport
• Biological source: Saccharomyces cerevisiae (yeast)
• Cellular location: Cytoplasm: Q12154
• Total number of polymer chains: 2
• Total formula weight: 81965.34

Authors

Yamagata, A.,Mimura, H.,Sato, Y.,Yamashita, M.,Yoshikawa, A.,Fukai, S. (deposition date: 2009-06-10, release date: 2010-01-12, Last modification date: 2024-03-13)

Primary citation

Yamagata, A.,Mimura, H.,Sato, Y.,Yamashita, M.,Yoshikawa, A.,Fukai, S.
Structural insight into the membrane insertion of tail-anchored proteins by Get3
Genes Cells, 15:29-41, 2010

PubMed Abstract: Tail anchored (TA) proteins, which are important for numerous cellular processes, are defined by a single transmembrane domain (TMD) near the C-terminus. The membrane insertion of TA proteins is mediated by the highly conserved ATPase Get3. Here we report the crystal structures of Get3 in ADP-bound and nucleotide-free forms at 3.0 A and 2.8 A resolutions, respectively. Get3 consists of a nucleotide binding domain and a helical domain. Both structures exhibit a Zn(2+)-mediated homodimer in a head-to-head orientation, representing an open dimer conformation. Our cross-link experiments indicated the closed dimer-stimulating ATP hydrolysis, which might be coupled with TA-protein release. Further, our coexpression-based binding assays using a model TA protein Sec22p revealed the direct interaction between the helical domain of Get3 and the Sec22p TMD. This interaction is independent of ATP and dimer formation. Finally, we propose a structural mechanism that links ATP hydrolysis with the TA-protein insertion mediated by the conserved DTAPTGH motif.

PubMed: 20015340
DOI: 10.1111/j.1365-2443.2009.01362.x

Experimental method

X-RAY DIFFRACTION (3 Å)