8PQX
p97 (VCP) mutant - F539A state III
Summary for 8PQX
| Entry DOI | 10.2210/pdb8pqx/pdb |
| EMDB information | 17827 |
| Descriptor | Transitional endoplasmic reticulum ATPase, ADENOSINE-5'-TRIPHOSPHATE, ADENOSINE-5'-DIPHOSPHATE (3 entities in total) |
| Functional Keywords | hexameric complex, atpase, unfoldase, protein quality control, segregase, chaperone |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 6 |
| Total formula weight | 541370.75 |
| Authors | Arie, M.,Matzov, D.,Karmona, R.,Szenkier, N.,Stanhill, A.,Navon, A. (deposition date: 2023-07-12, release date: 2024-05-29, Last modification date: 2024-12-25) |
| Primary citation | Arie, M.,Matzov, D.,Karmona, R.,Szenkier, N.,Stanhill, A.,Navon, A. A non-symmetrical p97 conformation initiates a multistep recruitment of Ufd1/Npl4. Iscience, 27:110061-110061, 2024 Cited by PubMed Abstract: experiments and cryo-EM structures of p97 and its cofactor, Ufd1/Npl4 (UN), elucidated substrate processing. Yet, the structural transitions and the related ATPase cycle upon UN binding remain unresolved. We captured two discrete conformations: One in which D1 protomers are ATP bound, while the D2 subunits are in the ADP state, presumably required for substrate engagement with the D2 pore; and a heterologous nucleotide state within the D1 ring in which only two NTDs are in the "up" ATP state that favors UN binding. Further analysis suggests that initially, UN binds p97's non-symmetrical conformation, this association promotes a structural transition upon which five NTDs shift to an "up" state and are poised to bind ATP. The UBXL domain of Npl4 was captured bound to an NTD in the ADP state, demonstrating a conformation that may provide directionality to incoming substrate and introduce the flexibility needed for substrate processing. PubMed: 38947518DOI: 10.1016/j.isci.2024.110061 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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