2A18
carboxysome shell protein ccmK4, crystal form 2
2A18 の概要
| エントリーDOI | 10.2210/pdb2a18/pdb |
| 関連するPDBエントリー | 2A10 2A1B |
| 分子名称 | Carbon dioxide concentrating mechanism protein ccmK homolog 4, AMMONIUM ION (3 entities in total) |
| 機能のキーワード | cyclic hexamer; c6 point symmetry, carboxysome |
| 由来する生物種 | Synechocystis sp. |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 40417.11 |
| 構造登録者 | Kerfeld, C.A.,Sawaya, M.R.,Tanaka, S.,Nguyen, C.V.,Phillips, M.,Beeby, M.,Yeates, T.O. (登録日: 2005-06-18, 公開日: 2005-08-09, 最終更新日: 2023-08-23) |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.28 Å) |
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