1R7R

The crystal structure of murine p97/VCP at 3.6A

1R7R の概要

• エントリーDOI: 10.2210/pdb1r7r/pdb
• 分子名称: Transitional endoplasmic reticulum ATPase, ADENOSINE-5'-DIPHOSPHATE (2 entities in total)
• 機能のキーワード: p97, vcp, aaa, cdc48, transport protein
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Cytoplasm, cytosol : Q01853
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 91063.31

構造登録者

Huyton, T.,Pye, V.E.,Briggs, L.C.,Flynn, T.C.,Beuron, F.,Kondo, H.,Ma, J.,Zhang, X.,Freemont, P.S. (登録日: 2003-10-22, 公開日: 2003-12-16, 最終更新日: 2023-08-23)

主引用文献

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

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: 14643202
DOI: 10.1016/j.jsb.2003.10.007

実験手法

X-RAY DIFFRACTION (3.6 Å)