9ly9 | pdb_00009ly9

Cryo-EM structure of carboxysomal mid-shell: T = 16 shell under C1 symmetry.

spinqualitylabelsall models 9ly9, resolution 3.71Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9ly9 is a 1080 chain structure with sequence from Halothiobacillus neapolitanus c2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.71Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CSOSA_HALNC The major shell protein of the carboxysome, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, ccbL-ccbS) is sequestered (PubMed:16535117, PubMed:7934888). Assembles into hexamers which make sheets that form the facets of the polyhedral carboxysome (PubMed:17518518). The shell probably limits the diffusion of CO(2) into and out of the carboxysome (Probable). Molecular modeling shows the central pore of this protein is selectively permeable to anions such as HCO(3) rather than CO(2) or O(2) (Probable). There are estimated to be 2970 CsoS1A/CsoS1C proteins per carboxysome (the proteins differ by only 1 residue) (Ref.5). Unlike beta-carboxysomes, alpha-carboxysomes (Cb) can form without cargo protein. CsoS2 is essential for Cb formation and is also capable of targeting foreign proteins to the Cb. The Cb shell assembles with the aid of CsoS2; CsoS1A, CsoS1B and CsoS1C form the majority of the shell while CsoS4A and CsoS4B form vertices. CsoS1D forms pseudohexamers that probably control metabolite flux into and out of the shell. Publication Abstract from PubMed Excessive symmetry in cryo-EM data processing can distort key structural details of bacterial microcompartments, highlighting the importance of balanced symmetry for accurate structural insights. Symmetry-adjusted cryo-EM analysis unveils the detailed linker protein CsoS2 interactions within the alpha-carboxysome shell.,Li J, Li T, Wang S, Zhang YZ, Liu LN, Wang P Plant Physiol. 2025 Apr 30;198(1):kiaf165. doi: 10.1093/plphys/kiaf165. PMID:40341945 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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