1wap: Difference between revisions

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{{STRUCTURE_1wap|  PDB=1wap  |  SCENE=  }}  
{{STRUCTURE_1wap|  PDB=1wap  |  SCENE=  }}  


'''TRP RNA-BINDING ATTENUATION PROTEIN IN COMPLEX WITH L-TRYPTOPHAN'''
===TRP RNA-BINDING ATTENUATION PROTEIN IN COMPLEX WITH L-TRYPTOPHAN===




==Overview==
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The crystal structure of the trp RNA-binding attenuation protein of Bacclius subtilis solved at 1.8 A resolution reveals a novel structural arrangement in which the eleven subunits are stabilized through eleven intersubunit beta-sheets to form a beta-wheel with a large central hole. The nature of the binding of L-tryptophan in clefts between adjacent beta-sheets in the beta-wheel suggests that this binding induces conformational changes in the flexible residues 25-33 and 49-52. It is argued that upon binding, the messenger RNA target forms a matching circle in which eleven U/GAG repeats are bound to the surface of the protein ondecamer modified by the binding of L-tryptophan.
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{{ABSTRACT_PUBMED_7715723}}


==About this Structure==
==About this Structure==
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[[Category: Bacillus subtili]]
[[Category: Bacillus subtili]]
[[Category: Trp operon]]
[[Category: Trp operon]]
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