1eyn: Difference between revisions

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[[Image:1eyn.jpg|left|200px]]
{{Seed}}
[[Image:1eyn.png|left|200px]]


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{{STRUCTURE_1eyn|  PDB=1eyn  |  SCENE=  }}  
{{STRUCTURE_1eyn|  PDB=1eyn  |  SCENE=  }}  


'''STRUCTURE OF MURA LIGANDED WITH THE EXTRINSIC FLUORESCENCE PROBE ANS'''
===STRUCTURE OF MURA LIGANDED WITH THE EXTRINSIC FLUORESCENCE PROBE ANS===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_10823915}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_10823915}}


==About this Structure==
==About this Structure==
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[[Category: Inside-out alpha-beta barrel]]
[[Category: Inside-out alpha-beta barrel]]
[[Category: L-isoaspartate in position 67]]
[[Category: L-isoaspartate in position 67]]
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