2A5F
Cholera toxin A1 subunit bound to its substrate, NAD+, and its human protein activator, ARF6
2A5F の概要
エントリーDOI | 10.2210/pdb2a5f/pdb |
分子名称 | ADP-ribosylation factor 6, Cholera enterotoxin, A chain, MAGNESIUM ION, ... (8 entities in total) |
機能のキーワード | protein transport/transferase, protein transport-transferase complex |
由来する生物種 | Homo sapiens (human) 詳細 |
細胞内の位置 | Golgi apparatus: P62330 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 43146.94 |
構造登録者 | O'Neal, C.J.,Jobling, M.G.,Holmes, R.K.,Hol, W.G.J. (登録日: 2005-06-30, 公開日: 2005-08-16, 最終更新日: 2024-04-03) |
主引用文献 | O'Neal, C.J.,Jobling, M.G.,Holmes, R.K.,Hol, W.G. Structural basis for the activation of cholera toxin by human ARF6-GTP. Science, 309:1093-1096, 2005 Cited by PubMed Abstract: The Vibrio cholerae bacterium causes devastating diarrhea when it infects the human intestine. The key event is adenosine diphosphate (ADP)-ribosylation of the human signaling protein GSalpha, catalyzed by the cholera toxin A1 subunit (CTA1). This reaction is allosterically activated by human ADP-ribosylation factors (ARFs), a family of essential and ubiquitous G proteins. Crystal structures of a CTA1:ARF6-GTP (guanosine triphosphate) complex reveal that binding of the human activator elicits dramatic changes in CTA1 loop regions that allow nicotinamide adenine dinucleotide (NAD+) to bind to the active site. The extensive toxin:ARF-GTP interface surface mimics ARF-GTP recognition of normal cellular protein partners, which suggests that the toxin has evolved to exploit promiscuous binding properties of ARFs. PubMed: 16099990DOI: 10.1126/science.1113398 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.02 Å) |
構造検証レポート
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