2A10
carboxysome shell protein ccmK4
Summary for 2A10
Entry DOI | 10.2210/pdb2a10/pdb |
Related | 2A18 2A1B |
Descriptor | Carbon dioxide concentrating mechanism protein ccmK homolog 4 (2 entities in total) |
Functional Keywords | cyclic hexamer; c6 point symmetry, carboxysome |
Biological source | Synechocystis sp. |
Total number of polymer chains | 6 |
Total formula weight | 80725.99 |
Authors | Kerfeld, C.A.,Sawaya, M.R.,Tanaka, S.,Nguyen, C.V.,Phillips, M.,Beeby, M.,Yeates, T.O. (deposition date: 2005-06-17, release date: 2005-08-09, Last modification date: 2024-02-14) |
Primary citation | Kerfeld, C.A.,Sawaya, M.R.,Tanaka, S.,Nguyen, C.V.,Phillips, M.,Beeby, M.,Yeates, T.O. Protein structures forming the shell of primitive bacterial organelles Science, 309:936-938, 2005 Cited by PubMed Abstract: Bacterial microcompartments are primitive organelles composed entirely of protein subunits. Genomic sequence databases reveal the widespread occurrence of microcompartments across diverse microbes. The prototypical bacterial microcompartment is the carboxysome, a protein shell for sequestering carbon fixation reactions. We report three-dimensional crystal structures of multiple carboxysome shell proteins, revealing a hexameric unit as the basic microcompartment building block and showing how these hexamers assemble to form flat facets of the polyhedral shell. The structures suggest how molecular transport across the shell may be controlled and how structural variations might govern the assembly and architecture of these subcellular compartments. PubMed: 16081736DOI: 10.1126/science.1113397 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.803 Å) |
Structure validation
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