3CF1

Structure of P97/vcp in complex with ADP/ADP.alfx

「1OZ4」から置き換えられました 「1YQ0」から置き換えられました

3CF1 の概要

• エントリーDOI: 10.2210/pdb3cf1/pdb
• 関連するPDBエントリー: 1OZ4 1YQ0 3CF2 3CF3
• 分子名称: Transitional endoplasmic reticulum ATPase, ADENOSINE-5'-DIPHOSPHATE, ALUMINUM FLUORIDE (3 entities in total)
• 機能のキーワード: aaa, cdc48, erad, atpase, 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: 3
• 化学式量合計: 271125.60

構造登録者

Davies, J.M.,Delabarre, B.,Brunger, A.T.,Weis, W.I. (登録日: 2008-03-01, 公開日: 2008-04-22, 最終更新日: 2024-02-21)

主引用文献

Davies, J.M.,Brunger, A.T.,Weis, W.I.
Improved structures of full-length p97, an AAA ATPase: implications for mechanisms of nucleotide-dependent conformational change.
Structure, 16:715-726, 2008

PubMed Abstract: The ATPases associated with various cellular activities (AAA) protein p97 has been implicated in a variety of cellular processes, including endoplasmic reticulum-associated degradation and homotypic membrane fusion. p97 belongs to a subgroup of AAA proteins that contains two nucleotide binding domains, D1 and D2. We determined the crystal structure of D2 at 3.0 A resolution. This model enabled rerefinement of full-length p97 in different nucleotide states against previously reported low-resolution diffraction data to significantly improved R values and Ramachandran statistics. Although the overall fold remained similar, there are significant improvements, especially around the D2 nucleotide binding site. The rerefinement illustrates the importance of knowledge of high-resolution structures of fragments covering most of the whole molecule. The structures suggest that nucleotide hydrolysis is transformed into larger conformational changes by pushing of one D2 domain by its neighbor in the hexamer, and transmission of nucleotide-state information through the D1-D2 linker to displace the N-terminal, effector binding domain.

PubMed: 18462676
DOI: 10.1016/j.str.2008.02.010

実験手法

X-RAY DIFFRACTION (4.4 Å)