7O4Z
Crystal structure of the carbonic anhydrase-like domain of CcmM from Synechococcus elongatus (strain PCC 7942)
7O4Z の概要
| エントリーDOI | 10.2210/pdb7o4z/pdb |
| 分子名称 | Carboxysome assembly protein CcmM, NICKEL (II) ION, CHLORIDE ION, ... (4 entities in total) |
| 機能のキーワード | protein binding carboxysome, photosynthesis |
| 由来する生物種 | Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans R2) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 19344.01 |
| 構造登録者 | |
| 主引用文献 | Zang, K.,Wang, H.,Hartl, F.U.,Hayer-Hartl, M. Scaffolding protein CcmM directs multiprotein phase separation in beta-carboxysome biogenesis. Nat.Struct.Mol.Biol., 28:909-922, 2021 Cited by PubMed Abstract: Carboxysomes in cyanobacteria enclose the enzymes Rubisco and carbonic anhydrase to optimize photosynthetic carbon fixation. Understanding carboxysome assembly has implications in agricultural biotechnology. Here we analyzed the role of the scaffolding protein CcmM of the β-cyanobacterium Synechococcus elongatus PCC 7942 in sequestrating the hexadecameric Rubisco and the tetrameric carbonic anhydrase, CcaA. We find that the trimeric CcmM, consisting of γCAL oligomerization domains and linked small subunit-like (SSUL) modules, plays a central role in mediation of pre-carboxysome condensate formation through multivalent, cooperative interactions. The γCAL domains interact with the C-terminal tails of the CcaA subunits and additionally mediate a head-to-head association of CcmM trimers. Interestingly, SSUL modules, besides their known function in recruiting Rubisco, also participate in intermolecular interactions with the γCAL domains, providing further valency for network formation. Our findings reveal the mechanism by which CcmM functions as a central organizer of the pre-carboxysome multiprotein matrix, concentrating the core components Rubisco and CcaA before β-carboxysome shell formation. PubMed: 34759380DOI: 10.1038/s41594-021-00676-5 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.67 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード
をダウンロード
