8HAC
A novel dimer configuration of a diatom Get3 forming a tetrameric complex with its tail-anchored membrane cargo
Summary for 8HAC
Entry DOI | 10.2210/pdb8hac/pdb |
Descriptor | ATPase ASNA1 homolog, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total) |
Functional Keywords | get3, arsa2, arsa1, trc40, tail-anchored, post-translational pathway, diatom, chaperone |
Biological source | Phaeodactylum tricornutum CCAP 1055/1 |
Total number of polymer chains | 2 |
Total formula weight | 78576.90 |
Authors | Chang, H.Y.,Ko, T.P. (deposition date: 2022-10-26, release date: 2024-05-15, Last modification date: 2024-06-26) |
Primary citation | Chen, C.C.,Huang, Y.R.,Chan, Y.T.,Lin, H.Y.,Lin, H.J.,Hsiao, C.D.,Ko, T.P.,Lin, T.W.,Lan, Y.H.,Lin, H.Y.,Chang, H.Y. A distinct dimer configuration of a diatom Get3 forming a tetrameric complex with its tail-anchored membrane cargo. Bmc Biol., 22:136-136, 2024 Cited by PubMed Abstract: Most tail-anchored (TA) membrane proteins are delivered to the endoplasmic reticulum through a conserved posttranslational pathway. Although core mechanisms underlying the targeting and insertion of TA proteins are well established in eukaryotes, their role in mediating TA protein biogenesis in plants remains unclear. We reported the crystal structures of algal arsenite transporter 1 (ArsA1), which possesses an approximately 80-kDa monomeric architecture and carries chloroplast-localized TA proteins. However, the mechanistic basis of ArsA2, a Get3 (guided entry of TA proteins 3) homolog in plants, for TA recognition remains unknown. PubMed: 38867239DOI: 10.1186/s12915-024-01933-x PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.32 Å) |
Structure validation
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