Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amino Acid Sequence
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Bacillus subtilis / chemistry
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Base Sequence
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Crystallography, X-Ray
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Models, Molecular
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Molecular Sequence Data
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Mutation
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Operon
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Protein Binding
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Protein Conformation
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Protein Structure, Secondary
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RNA, Messenger / metabolism
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RNA-Binding Proteins / chemistry*
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RNA-Binding Proteins / genetics
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RNA-Binding Proteins / metabolism
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Sequence Homology, Amino Acid
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Transcription Factors / chemistry*
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Transcription Factors / genetics
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Transcription Factors / metabolism
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Tryptophan / genetics
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Tryptophan / metabolism
Substances
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Bacterial Proteins
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MtrB protein, Bacteria
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RNA, Messenger
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RNA-Binding Proteins
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Transcription Factors
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Tryptophan