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2EWS

Crystal structure of S.aureus pantothenate kinase

2EWS の概要
エントリーDOI10.2210/pdb2ews/pdb
分子名称Pantothenate kinase, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total)
機能のキーワードpank, structural genomics, structural genomics consortium, sgc, transferase
由来する生物種Staphylococcus aureus subsp. aureus
タンパク質・核酸の鎖数2
化学式量合計63657.60
構造登録者
Hong, B.S.,Park, H.W.,Structural Genomics Consortium (SGC) (登録日: 2005-11-06, 公開日: 2006-09-12, 最終更新日: 2024-02-14)
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: 16905099
DOI: 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 (2.05 Å)
構造検証レポート
Validation report summary of 2ews
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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