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          Institute: MPI für medizinische Forschung     Collection: Abteilung Biophysik     Display Documents

ID: 22830.0, MPI für medizinische Forschung / Abteilung Biophysik
Structural basis for the interaction of the fluorescence probe 8-anilino-1-naphthalene sulfonate (ANS) with the antibiotic target MurA
Translation of Title:Structural basis for the interaction of the fluorescence probe 8-anilino-1-naphthalene sulfonate (ANS) with the antibiotic target MurA
Authors:Schönbrunn, Ernst; Eschenburg, Susanne; Luger, Karolin; Kabsch, Wolfgang; Amrhein, Nikolaus
Date of Publication (YYYY-MM-DD):2000-06-06
Title of Journal:Proceedings of the National Academy of Sciences of the United States of America
Journal Abbrev.:Proceedings of the National Academy of Sciences of
Issue / Number:12
Start Page:6345
End Page:6349
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description: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?MurA complex at 1.7-? 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.
External Publication Status:published
Document Type:Article
Communicated by:Wulf Kaiser
Affiliations:MPI für medizinische Forschung/Abteilung Biophysik/
Identifiers:URI: [Full text]
URI: [Abstract]
URI: [Fulltext PDF]
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