村上
化学
荧光
基质(水族馆)
立体化学
酶
磺酸盐
结合位点
生物物理学
构象变化
晶体结构
结晶学
生物化学
生物
有机化学
操作系统
物理
液晶显示器
量子力学
钠
计算机科学
生态学
作者
E. Schönbrunn,Susanne Eschenburg,Karolin Luger,Wolfgang Kabsch,Nikolaus Amrhein
标识
DOI:10.1073/pnas.120120397
摘要
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 enol pyruvyltransferase (EC 2.5.1.7 )], an essential enzyme for bacterial cell wall biosynthesis. We have solved the crystal structure of the ANS⋅MurA complex at 1.7-Å 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.
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