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6J7F

Complex of GGTaseIII, farnesyl-Ykt6 (C-terminal methylated), and GGPP

Summary for 6J7F
Entry DOI10.2210/pdb6j7f/pdb
DescriptorProtein prenyltransferase alpha subunit repeat-containing protein 1, Geranylgeranyl transferase type-2 subunit beta, Synaptobrevin homolog YKT6, ... (7 entities in total)
Functional Keywordslipid transferase, lipid binding protein
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains3
Total formula weight98308.30
Authors
Goto-Ito, S.,Yamagata, A.,Sato, Y.,Fukai, S. (deposition date: 2019-01-18, release date: 2020-01-22, Last modification date: 2025-05-28)
Primary citationShirakawa, R.,Goto-Ito, S.,Goto, K.,Wakayama, S.,Kubo, H.,Sakata, N.,Trinh, D.A.,Yamagata, A.,Sato, Y.,Masumoto, H.,Cheng, J.,Fujimoto, T.,Fukai, S.,Horiuchi, H.
A SNARE geranylgeranyltransferase essential for the organization of the Golgi apparatus.
Embo J., 39:e104120-e104120, 2020
Cited by
PubMed Abstract: Protein prenylation is essential for many cellular processes including signal transduction, cytoskeletal reorganization, and membrane trafficking. Here, we identify a novel type of protein prenyltransferase, which we named geranylgeranyltransferase type-III (GGTase-III). GGTase-III consists of prenyltransferase alpha subunit repeat containing 1 (PTAR1) and the β subunit of RabGGTase. Using a biotinylated geranylgeranyl analogue, we identified the Golgi SNARE protein Ykt6 as a substrate of GGTase-III. GGTase-III transfers a geranylgeranyl group to mono-farnesylated Ykt6, generating doubly prenylated Ykt6. The crystal structure of GGTase-III in complex with Ykt6 provides structural basis for Ykt6 double prenylation. In GGTase-III-deficient cells, Ykt6 remained in a singly prenylated form, and the Golgi SNARE complex assembly was severely impaired. Consequently, the Golgi apparatus was structurally disorganized, and intra-Golgi protein trafficking was delayed. Our findings reveal a fourth type of protein prenyltransferase that generates geranylgeranyl-farnesyl Ykt6. Double prenylation of Ykt6 is essential for the structural and functional organization of the Golgi apparatus.
PubMed: 32128853
DOI: 10.15252/embj.2019104120
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.883 Å)
Structure validation

238895

건을2025-07-16부터공개중

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