1qaw
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(New page: 200px<br /><applet load="1qaw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qaw, resolution 2.5Å" /> '''REGULATORY FEATURES O...)
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Revision as of 22:25, 20 November 2007
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REGULATORY FEATURES OF THE TRP OPERON AND THE CRYSTAL STRUCTURE OF THE TRP RNA-BINDING ATTENUATION PROTEIN FROM BACILLUS STEAROTHERMOPHILUS.
Overview
Characterization of both the cis and trans -acting regulatory elements, indicates that the Bacillus stearothermophilustrp operon is regulated by, an attenuation mechanism similar to that which controls the trp operon in, Bacillus subtilis. Secondary structure predictions indicate that the, leader region of the trp mRNA is capable of folding into terminator and, anti- terminator RNA structures. B. stearothermophilus also encodes an, RNA-binding protein with 77% sequence identity with the RNA-binding, protein (TRAP) that regulates attenuation in B. subtilis. The X-ray, structure of this protein has been determined in complex with L-tryptophan, at 2.5 A resolution. Like the B. subtilis protein, B. stearothermophilus, TRAP has 11 subunits arranged in a ring-like structure. The central, cavities in these two structures have different sizes and opposite charge, distributions, and packing within the B. stearothermophilus TRAP crystal, form does not generate the head-to-head dimers seen in the B. subtilis, protein, suggesting that neither of these properties is functionally, important. However, the mode of L-tryptophan binding and the proposed RNA, binding surfaces are similar, indicating that both proteins are activated, by l -tryptophan and bind RNA in essentially the same way. As expected, the TRAP:RNA complex from B. stearothermophilus is significantly more, thermostable than that from B. subtilis, with optimal binding occurring at, 70 degrees C.
About this Structure
1QAW is a Single protein structure of sequence from Geobacillus stearothermophilus with TRP as ligand. Full crystallographic information is available from OCA.
Reference
Regulatory features of the trp operon and the crystal structure of the trp RNA-binding attenuation protein from Bacillus stearothermophilus., Chen X, Antson AA, Yang M, Li P, Baumann C, Dodson EJ, Dodson GG, Gollnick P, J Mol Biol. 1999 Jun 18;289(4):1003-16. PMID:10369778
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