4UPF

Assembly principles of the unique cage formed by the ATPase RavA hexamer and the lysine decarboxylase LdcI decamer

4UPF の概要

• エントリーDOI: 10.2210/pdb4upf/pdb
• 関連するPDBエントリー: 4UPB
• EMDBエントリー: 2681
• 分子名称: LYSINE DECARBOXYLASE, INDUCIBLE, ATPASE RAVA (2 entities in total)
• 機能のキーワード: lyase-hydrolase complex, lysine decarboxylase, aaa+ atpase, acid stress response, lyase/hydrolase
• 由来する生物種: ESCHERICHIA COLI STR. K-12 SUBSTR. MG1655; 詳細
• 細胞内の位置: Cytoplasm : P0A9H3 P31473
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 93976.47

構造登録者

Malet, H.,Liu, K.,El Bakkouri, M.,Chan, S.W.S.,Effantin, G.,Bacia, M.,Houry, W.A.,Gutsche, I. (登録日: 2014-06-16, 公開日: 2014-08-20, 最終更新日: 2024-05-08)

主引用文献

Malet, H.,Liu, K.,El Bakkouri, M.,Chan, S.W.S.,Effantin, G.,Bacia, M.,Houry, W.A.,Gutsche, I.
Assembly Principles of a Unique Cage Formed by Hexameric and Decameric E. Coli Proteins.
Elife, 3:03653-, 2014

PubMed Abstract: A 3.3 MDa macromolecular cage between two Escherichia coli proteins with seemingly incompatible symmetries-the hexameric AAA+ ATPase RavA and the decameric inducible lysine decarboxylase LdcI-is reconstructed by cryo-electron microscopy to 11 Å resolution. Combined with a 7.5 Å resolution reconstruction of the minimal complex between LdcI and the LdcI-binding domain of RavA, and the previously solved crystal structures of the individual components, this work enables to build a reliable pseudoatomic model of this unusual architecture and to identify conformational rearrangements and specific elements essential for complex formation. The design of the cage created via lateral interactions between five RavA rings is unique for the diverse AAA+ ATPase superfamily.

PubMed: 25097238
DOI: 10.7554/ELIFE.03653

実験手法

ELECTRON MICROSCOPY (7.5 Å)