5NV3

Structure of Rubisco from Rhodobacter sphaeroides in complex with CABP

5NV3 の概要

• エントリーDOI: 10.2210/pdb5nv3/pdb
• EMDBエントリー: 3699
• 分子名称: Ribulose bisphosphate carboxylase large chain, Ribulose bisphosphate carboxylase small chain 1, 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: beta barrel, lyase
• 由来する生物種: Rhodobacter sphaeroides; 詳細
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 538660.05

構造登録者

Bracher, A.,Milicic, G.,Ciniawsky, S.,Wendler, P.,Hayer-Hartl, M.,Hartl, F.U. (登録日: 2017-05-03, 公開日: 2017-07-26, 最終更新日: 2025-04-09)

主引用文献

Bhat, J.Y.,Milicic, G.,Thieulin-Pardo, G.,Bracher, A.,Maxwell, A.,Ciniawsky, S.,Mueller-Cajar, O.,Engen, J.R.,Hartl, F.U.,Wendler, P.,Hayer-Hartl, M.
Mechanism of Enzyme Repair by the AAA(+) Chaperone Rubisco Activase.
Mol. Cell, 67:744-756.e6, 2017

PubMed Abstract: How AAA+ chaperones conformationally remodel specific target proteins in an ATP-dependent manner is not well understood. Here, we investigated the mechanism of the AAA+ protein Rubisco activase (Rca) in metabolic repair of the photosynthetic enzyme Rubisco, a complex of eight large (RbcL) and eight small (RbcS) subunits containing eight catalytic sites. Rubisco is prone to inhibition by tight-binding sugar phosphates, whose removal is catalyzed by Rca. We engineered a stable Rca hexamer ring and analyzed its functional interaction with Rubisco. Hydrogen/deuterium exchange and chemical crosslinking showed that Rca structurally destabilizes elements of the Rubisco active site with remarkable selectivity. Cryo-electron microscopy revealed that Rca docks onto Rubisco over one active site at a time, positioning the C-terminal strand of RbcL, which stabilizes the catalytic center, for access to the Rca hexamer pore. The pulling force of Rca is fine-tuned to avoid global destabilization and allow for precise enzyme repair.

PubMed: 28803776
DOI: 10.1016/j.molcel.2017.07.004

実験手法

ELECTRON MICROSCOPY (3.39 Å)