6JY5
Structure of CsoS4B from Halothiobacillus neapolitanus
Summary for 6JY5
| Entry DOI | 10.2210/pdb6jy5/pdb |
| Descriptor | Unidentified carboxysome polypeptide (2 entities in total) |
| Functional Keywords | carboxysome shell protein, pentameric protein, structural protein |
| Biological source | Halothiobacillus neapolitanus |
| Total number of polymer chains | 5 |
| Total formula weight | 46588.70 |
| Authors | Zhao, Y.Y.,Jiang, Y.L.,Chen, Y.,Zhou, C.Z.,Li, Q. (deposition date: 2019-04-26, release date: 2019-06-26, Last modification date: 2023-11-22) |
| Primary citation | Zhao, Y.Y.,Jiang, Y.L.,Chen, Y.,Zhou, C.Z.,Li, Q. Crystal structure of pentameric shell protein CsoS4B of Halothiobacillus neapolitanus alpha-carboxysome. Biochem.Biophys.Res.Commun., 515:510-515, 2019 Cited by PubMed Abstract: Carboxysome, encapsulating an enzymatic core within an icosahedral-shaped semipermeable protein shell, could enhance CO fixation under low CO conditions in the environment. The shell of Halothiobacillus neapolitanus α-carboxysome possesses two 38% sequence-identical pentameric proteins, namely CsoS4A and CsoS4B. However, the functions of two paralogous pentameric proteins in α-carboxysome assembly remain unknown. Here we report the crystal structure of CsoS4B at 2.15 Å resolution. It displays as a stable pentamer, each subunit of which consists of a β-barrel core domain, in addition to an insertion of helix α1 that forms the central pore. Structural comparisons and multiple-sequence alignment strongly indicate that CsoS4A and CsoS4B differ from each other in interacting with various components of α-carboxysome, despite they share a similar overall structure. These findings provide the structural basis for further investigations on the self-assembly process of carboxysome. PubMed: 31171360DOI: 10.1016/j.bbrc.2019.05.047 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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