7D6C
Crystal structure of CcmM N-terminal domain in complex with CcmN
Summary for 7D6C
| Entry DOI | 10.2210/pdb7d6c/pdb |
| Descriptor | Carbon dioxide concentrating mechanism protein CcmM, Carboxysome assembly protein CcmN (3 entities in total) |
| Functional Keywords | co2-concentrating mechanism, carboxysome, scaffolding protein, complex, structural protein |
| Biological source | Synechococcus elongatus (strain PCC 7942 / FACHB-805) More |
| Total number of polymer chains | 6 |
| Total formula weight | 94851.99 |
| Authors | Sun, H.,Cui, N.,Han, S.J.,Chen, Z.P.,Xia, L.Y.,Chen, Y.,Jiang, Y.L.,Zhou, C.Z. (deposition date: 2020-09-30, release date: 2021-08-04, Last modification date: 2023-11-29) |
| Primary citation | 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 Cited by 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: 33928692DOI: 10.1002/pro.4090 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.89 Å) |
Structure validation
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