Abstract
Anti-TRAP protein regulates the expression of tryptophan biosynthetic genes by binding to TRAP and preventing formation of the TRAP-RNA complex. Anti-TRAP from Bacillus subtilis has been crystallized by vapour diffusion. The crystals belong to space group P1, with unit-cell parameters a = 51.6, b = 60.1, c = 60.4 A, alpha = 114.0, beta = 101.4, gamma = 100.5 degrees. X-ray data have been collected to 2.8 A resolution. Peaks in the self-rotation function correspond to four trimers in the unit cell related by twofold and threefold rotational axes. The symmetry and gel-filtration data suggest that the protein exists as a trimer or a dodecamer in solution.
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.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Bacillus subtilis / chemistry*
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Bacterial Proteins / chemistry*
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Bacterial Proteins / isolation & purification
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Bacterial Proteins / metabolism
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Crystallization
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Crystallography, X-Ray
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RNA-Binding Proteins / chemistry*
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RNA-Binding Proteins / isolation & purification
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RNA-Binding Proteins / metabolism
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Stereoisomerism
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Transcription Factors / chemistry*
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Transcription Factors / isolation & purification
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Transcription Factors / metabolism
Substances
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Bacterial Proteins
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RNA-Binding Proteins
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Transcription Factors
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yczA protein, Bacillus subtilis