2D1G

Structure of Francisella tularensis Acid Phosphatase A (AcpA) bound to orthovanadate

2D1G の概要

• エントリーDOI: 10.2210/pdb2d1g/pdb
• 分子名称: acid phosphatase, VANADATE ION, UNKNOWN ATOM OR ION, ... (8 entities in total)
• 機能のキーワード: francisella tularensis, acid phosphatase, acpa, decavanadate, vanadate, hydrolase
• 由来する生物種: Francisella tularensis subsp. novicida
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 114463.50

構造登録者

Felts, R.L.,Reilly, T.J.,Tanner, J.J. (登録日: 2005-08-20, 公開日: 2006-08-15, 最終更新日: 2024-10-16)

主引用文献

Felts, R.L.,Reilly, T.J.,Tanner, J.J.
Structure of Francisella tularensis AcpA: prototype of a unique superfamily of acid phosphatases and phospholipases C
J.Biol.Chem., 281:30289-30298, 2006

PubMed Abstract: AcpA is a respiratory burst-inhibiting acid phosphatase from the Centers for Disease Control and Prevention Category A bioterrorism agent Francisella tularensis and prototype of a superfamily of acid phosphatases and phospholipases C. We report the 1.75-A resolution crystal structure of AcpA complexed with the inhibitor orthovanadate, which is the first structure of any F. tularensis protein and the first for any member of this superfamily. The core domain is a twisted 8-stranded beta-sheet flanked by three alpha-helices on either side, with the active site located above the carboxyl-terminal edge of the beta-sheet. This architecture is unique among acid phosphatases and resembles that of alkaline phosphatase. Unexpectedly, the active site features a serine nucleophile and metal ion with octahedral coordination. Structure-based sequence analysis of the AcpA superfamily predicts that the hydroxyl nucleophile and metal center are also present in AcpA-like phospholipases C. These results imply a phospholipase C catalytic mechanism that is radically different from that of zinc metallophospholipases.

PubMed: 16899453
DOI: 10.1074/jbc.M606391200

実験手法

X-RAY DIFFRACTION (1.75 Å)