6O60
Crystal structure of GGTase3-FBXL2-SKP1 complex
Summary for 6O60
| Entry DOI | 10.2210/pdb6o60/pdb |
| Descriptor | Protein prenyltransferase alpha subunit repeat-containing protein 1, Geranylgeranyl transferase type-2 subunit beta, F-box/LRR-repeat protein 2, ... (6 entities in total) |
| Functional Keywords | f-box, leucine-rich repeat, ggtase subunits, transferase |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 149901.83 |
| Authors | |
| Primary citation | Kuchay, S.,Wang, H.,Marzio, A.,Jain, K.,Homer, H.,Fehrenbacher, N.,Philips, M.R.,Zheng, N.,Pagano, M. GGTase3 is a newly identified geranylgeranyltransferase targeting a ubiquitin ligase. Nat.Struct.Mol.Biol., 26:628-636, 2019 Cited by PubMed Abstract: Protein prenylation is believed to be catalyzed by three heterodimeric enzymes: FTase, GGTase1 and GGTase2. Here we report the identification of a previously unknown human prenyltransferase complex consisting of an orphan prenyltransferase α-subunit, PTAR1, and the catalytic β-subunit of GGTase2, RabGGTB. This enzyme, which we named GGTase3, geranylgeranylates FBXL2 to allow its localization at cell membranes, where this ubiquitin ligase mediates the polyubiquitylation of membrane-anchored proteins. In cells, FBXL2 is specifically recognized by GGTase3 despite having a typical carboxy-terminal CaaX prenylation motif that is predicted to be recognized by GGTase1. Our crystal structure analysis of the full-length GGTase3-FBXL2-SKP1 complex reveals an extensive multivalent interface specifically formed between the leucine-rich repeat domain of FBXL2 and PTAR1, which unmasks the structural basis of the substrate-enzyme specificity. By uncovering a missing prenyltransferase and its unique mode of substrate recognition, our findings call for a revision of the 'prenylation code'. PubMed: 31209342DOI: 10.1038/s41594-019-0249-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.503 Å) |
Structure validation
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