5GJQ
Structure of the human 26S proteasome bound to USP14-UbAl
Summary for 5GJQ
| Entry DOI | 10.2210/pdb5gjq/pdb |
| Related | 5GJR |
| EMDB information | 9507 9508 9509 9510 9511 9512 |
| Descriptor | Proteasome subunit beta type-6, Proteasome subunit alpha type-5, Proteasome subunit beta type-1, ... (35 entities in total) |
| Functional Keywords | protein complex, human proteasome, hydrolase |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 48 |
| Total formula weight | 1730310.81 |
| Authors | Huang, X.L.,Luan, B.,Wu, J.P.,Shi, Y.G. (deposition date: 2016-07-01, release date: 2016-08-17, Last modification date: 2019-11-06) |
| Primary citation | Huang, X.,Luan, B.,Wu, J.,Shi, Y. An atomic structure of the human 26S proteasome. Nat. Struct. Mol. Biol., 23:778-785, 2016 Cited by PubMed Abstract: We report the cryo-EM structure of the human 26S proteasome at an average resolution of 3.5 Å, allowing atomic modeling of 28 subunits in the core particle (CP) and 18 subunits in the regulatory particle (RP). The C-terminal residues of Rpt3 and Rpt5 subunits in the RP can be seen inserted into surface pockets formed between adjacent α subunits in the CP. Each of the six Rpt subunits contains a bound nucleotide, and the central gate of the CP α-ring is closed despite RP association. The six pore 1 loops in the Rpt ring are arranged similarly to a spiral staircase along the axial channel of substrate transport, which is constricted by the pore 2 loops. We also determined the cryo-EM structure of the human proteasome bound to the deubiquitinating enzyme USP14 at 4.35-Å resolution. Together, our structures provide a framework for mechanistic understanding of eukaryotic proteasome function. PubMed: 27428775DOI: 10.1038/nsmb.3273 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.5 Å) |
Structure validation
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