1PTA

THREE-DIMENSIONAL STRUCTURE OF PHOSPHOTRIESTERASE: AN ENZYME CAPABLE OF DETOXIFYING ORGANOPHOSPHATE NERVE AGENTS

1PTA の概要

• エントリーDOI: 10.2210/pdb1pta/pdb
• 分子名称: PHOSPHOTRIESTERASE (2 entities in total)
• 機能のキーワード: hydrolase (organophosphate-degrading)
• 由来する生物種: Brevundimonas diminuta
• 細胞内の位置: Cell membrane; Peripheral membrane protein: P0A434
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35486.52

構造登録者

Benning, M.,Holden, H.M. (登録日: 1994-07-07, 公開日: 1995-12-01, 最終更新日: 2024-02-14)

主引用文献

Benning, M.M.,Kuo, J.M.,Raushel, F.M.,Holden, H.M.
Three-dimensional structure of phosphotriesterase: an enzyme capable of detoxifying organophosphate nerve agents.
Biochemistry, 33:15001-15007, 1994

PubMed Abstract: Organophosphates, such as parathion and paraoxon, constitute the largest class of insecticides currently used in industrialized nations. In addition, many of these compounds are known to inhibit mammalian acetylcholinesterases thereby acting as nerve agents. Consequently, organophosphate-degrading enzymes are of considerable interest in light of their ability to detoxify such compounds. Here we report the three-dimensional structure of such an enzyme, namely, phosphotriesterase, as determined by single crystal X-ray diffraction analysis to 2.1-A resolution. Crystals employed in this investigation belonged to the space group P2(1)2(1)2 with unit cell dimensions of a = 80.3 A, b = 93.4 A, and c = 44.8 A and one molecule per asymmetric unit. The structure was solved by multiple isomorphous replacement with two heavy-atom derivatives and refined to a crystallographic R factor of 18.0%. As observed in various other enzymes, the overall fold of the molecule consists of an alpha/beta barrel with eight strands of parallel beta-pleated sheet. In addition, there are two antiparallel beta-strands at the N-terminus. The molecular model of phosphotriesterase presented here provides the initial structural framework necessary toward understanding the enzyme's broad substrate specificities and its catalytic mechanism.

PubMed: 7999757
DOI: 10.1021/bi00254a008

実験手法

X-RAY DIFFRACTION (2.1 Å)