1R7R
The crystal structure of murine p97/VCP at 3.6A
Summary for 1R7R
| Entry DOI | 10.2210/pdb1r7r/pdb |
| Descriptor | Transitional endoplasmic reticulum ATPase, ADENOSINE-5'-DIPHOSPHATE (2 entities in total) |
| Functional Keywords | p97, vcp, aaa, cdc48, transport protein |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Cytoplasm, cytosol : Q01853 |
| Total number of polymer chains | 1 |
| Total formula weight | 91063.31 |
| Authors | Huyton, T.,Pye, V.E.,Briggs, L.C.,Flynn, T.C.,Beuron, F.,Kondo, H.,Ma, J.,Zhang, X.,Freemont, P.S. (deposition date: 2003-10-22, release date: 2003-12-16, Last modification date: 2023-08-23) |
| Primary citation | Huyton, T.,Pye, V.E.,Briggs, L.C.,Flynn, T.C.,Beuron, F.,Kondo, H.,Ma, J.,Zhang, X.,Freemont, P.S. The crystal structure of murine p97/VCP at 3.6A J.Struct.Biol., 144:337-348, 2003 Cited by PubMed Abstract: p97/VCP is a member of the AAA ATPase family and has roles in both membrane fusion and ubiquitin dependent protein degradation. Here, we present a 3.6A crystal structure of murine p97 in which D2 domain has been modelled as poly-alanine and the remaining approximately 100 residues are absent. The resulting structure illustrates a head-to-tail packing arrangement of the two p97 AAA domains in a natural hexameric state with D1 ADP bound and D2 nucleotide free. The head-to-tail packing arrangement observed in this structure is in contrast to our previously predicted tail-to-tail packing model. The linker between the D1 and D2 domains is partially disordered, suggesting a flexible nature. Normal mode analysis of the crystal structure suggests anti-correlated motions and distinct conformational states of the two AAA domains. PubMed: 14643202DOI: 10.1016/j.jsb.2003.10.007 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.6 Å) |
Structure validation
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