2F9W
Structure of the type III CoaA from Pseudomonas aeruginosa
2F9W の概要
| エントリーDOI | 10.2210/pdb2f9w/pdb |
| 関連するPDBエントリー | 2F9T |
| 分子名称 | Pantothenate Kinase, PANTOTHENOIC ACID, 1,2-ETHANEDIOL, ... (5 entities in total) |
| 機能のキーワード | pantothenate kinase, coaa, pan, pantothenate, transferase |
| 由来する生物種 | Pseudomonas aeruginosa |
| 細胞内の位置 | Cytoplasm (By similarity): Q9HWC1 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 59900.36 |
| 構造登録者 | Leonardi, R.,Yun, M.K.,Chohnan, S.,White, S.W.,Rock, C.O.,Jackowski, S. (登録日: 2005-12-06, 公開日: 2006-08-22, 最終更新日: 2024-10-30) |
| 主引用文献 | Hong, B.S.,Yun, M.K.,Zhang, Y.M.,Chohnan, S.,Rock, C.O.,White, S.W.,Jackowski, S.,Park, H.W.,Leonardi, R. Prokaryotic Type II and Type III Pantothenate Kinases: The Same Monomer Fold Creates Dimers with Distinct Catalytic Properties. Structure, 14:1251-1261, 2006 Cited by PubMed Abstract: Three distinct isoforms of pantothenate kinase (CoaA) in bacteria catalyze the first step in coenzyme A biosynthesis. The structures of the type II (Staphylococcus aureus, SaCoaA) and type III (Pseudomonas aeruginosa, PaCoaA) enzymes reveal that they assemble nearly identical subunits with actin-like folds into dimers that exhibit distinct biochemical properties. PaCoaA has a fully enclosed pantothenate binding pocket and requires a monovalent cation to weakly bind ATP in an open cavity that does not interact with the adenine nucleotide. Pantothenate binds to an open pocket in SaCoaA that strongly binds ATP by using a classical P loop architecture coupled with specific interactions with the adenine moiety. The PaCoaA*Pan binary complex explains the resistance of bacteria possessing this isoform to the pantothenamide antibiotics, and the similarity between SaCoaA and human pantothenate kinase 2 explains the molecular basis for the development of the neurodegenerative phenotype in three mutations in the human protein. PubMed: 16905099DOI: 10.1016/j.str.2006.06.008 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.9 Å) |
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