7D6C

Crystal structure of CcmM N-terminal domain in complex with CcmN

7D6C の概要

• エントリーDOI: 10.2210/pdb7d6c/pdb
• 分子名称: Carbon dioxide concentrating mechanism protein CcmM, Carboxysome assembly protein CcmN (3 entities in total)
• 機能のキーワード: co2-concentrating mechanism, carboxysome, scaffolding protein, complex, structural protein
• 由来する生物種: Synechococcus elongatus (strain PCC 7942 / FACHB-805); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 94851.99

構造登録者

Sun, H.,Cui, N.,Han, S.J.,Chen, Z.P.,Xia, L.Y.,Chen, Y.,Jiang, Y.L.,Zhou, C.Z. (登録日: 2020-09-30, 公開日: 2021-08-04, 最終更新日: 2023-11-29)

主引用文献

Sun, H.,Cui, N.,Han, S.J.,Chen, Z.P.,Xia, L.Y.,Chen, Y.,Jiang, Y.L.,Zhou, C.Z.
Complex structure reveals CcmM and CcmN form a heterotrimeric adaptor in beta-carboxysome.
Protein Sci., 30:1566-1576, 2021

PubMed Abstract: Carboxysome is an icosahedral self-assembled microcompartment that sequesters RuBisCO and carbonic anhydrases within a selectively permeable protein shell. The scaffolding proteins, CcmM, and CcmN were proposed to act as adaptors that crosslink the enzymatic core to shell facets. However, the details of interaction pattern remain unknown. Here we obtained a stable heterotrimeric complex of CcmM γ-carbonic anhydrase domain (termed CcmM ) and CcmN, with a 1:2 stoichiometry, which interacts with the shell proteins CcmO and CcmL in vitro. The 2.9 Å crystal structure of this heterotrimer revealed an asymmetric bundle composed of one CcmM and two CcmN subunits, all of which adopt a triangular left-handed β-helical barrel structure. The central CcmN subunit packs against CcmM and another CcmN subunit via a wall-to-edge or wall-to-wall pattern, respectively. Together with previous findings, we propose CcmM -CcmN functions as an adaptor to facilitate the recruitment of shell proteins and the assembly of intact β-carboxysome.

PubMed: 33928692
DOI: 10.1002/pro.4090

実験手法

X-RAY DIFFRACTION (2.89 Å)