Anti-TRAP protein from Bacillus subtilis: crystallization and internal symmetry.
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.
Shevtsov
Mikhail B
MB
York Structural Biology Laboratory, Chemistry Department, York University, York YO10 5YW, England.
Chen
Yanling
Y
Gollnick
Paul
P
Antson
Alfred A
AA
D001412:Bacillus subtilis / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D013237:Stereoisomerism; D014157:Transcription Factors / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism
D001426:Bacterial Proteins; D016601:RNA-Binding Proteins; D014157:Transcription Factors; C435924:yczA protein, Bacillus subtilis