1eyn
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(New page: 200px<br /><applet load="1eyn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eyn, resolution 1.7Å" /> '''STRUCTURE OF MURA LIG...)
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Revision as of 12:19, 20 November 2007
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STRUCTURE OF MURA LIGANDED WITH THE EXTRINSIC FLUORESCENCE PROBE ANS
Overview
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.
About this Structure
1EYN is a Single protein structure of sequence from Enterobacter cloacae with 2AN and GOL as ligands. Active as UDP-N-acetylglucosamine 1-carboxyvinyltransferase, with EC number 2.5.1.7 Full crystallographic information is available from OCA.
Reference
Structural basis for the interaction of the fluorescence probe 8-anilino-1-naphthalene sulfonate (ANS) with the antibiotic target MurA., Schonbrunn E, Eschenburg S, Luger K, Kabsch W, Amrhein N, Proc Natl Acad Sci U S A. 2000 Jun 6;97(12):6345-9. PMID:10823915
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