1EYN

Structure of mura liganded with the extrinsic fluorescence probe ANS

1EYN の概要

• エントリーDOI: 10.2210/pdb1eyn/pdb
• 関連するPDBエントリー: 1DLG 1EJC 1EJD 1NAW
• 分子名称: UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYLTRANSFERASE, 8-ANILINO-1-NAPHTHALENE SULFONATE, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: inside-out alpha-beta barrel; l-isoaspartate in position 67, transferase
• 由来する生物種: Enterobacter cloacae
• 細胞内の位置: Cytoplasm (Probable): P33038
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 45312.94

構造登録者

Schonbrunn, E.,Eschenburg, S.,Luger, K.,Kabsch, W.,Amrhein, N. (登録日: 2000-05-07, 公開日: 2000-06-09, 最終更新日: 2024-10-30)

主引用文献

Schonbrunn, E.,Eschenburg, S.,Luger, K.,Kabsch, W.,Amrhein, N.
Structural basis for the interaction of the fluorescence probe 8-anilino-1-naphthalene sulfonate (ANS) with the antibiotic target MurA.
Proc.Natl.Acad.Sci.USA, 97:6345-6349, 2000

PubMed Abstract: The extrinsic fluorescence dye 8-anilino-1-naphthalene sulfonate (ANS) is widely used for probing conformational changes in proteins, yet no detailed structure of ANS bound to any protein has been reported so far. ANS has been successfully used to monitor the induced-fit mechanism of MurA [UDPGlcNAc enolpyruvyltransferase (EC )], an essential enzyme for bacterial cell wall biosynthesis. We have solved the crystal structure of the ANS small middle dotMurA complex at 1.7-A resolution. ANS binds at an originally solvent-exposed region near Pro-112 and induces a major restructuring of the loop Pro-112-Pro-121, such that a specific binding site emerges. The fluorescence probe is sandwiched between the strictly conserved residues Arg-91, Pro-112, and Gly-113. Substrate binding to MurA is accompanied by large movements especially of the loop and Arg-91, which explains why ANS is an excellent sensor of conformational changes during catalysis of this pharmaceutically important enzyme.

PubMed: 10823915
DOI: 10.1073/pnas.120120397

実験手法

X-RAY DIFFRACTION (1.7 Å)