1.6.99.1 | more |
the enzyme shows a classical (alpha/beta)8 fold with the FMN prosthetic group buried at the positively-charged active-site cleft. In solution, TcOYE behaves as a globular monomer, but it exhibits a molecular envelope larger than that observed in the crystal structure, suggesting intrinsic protein flexibility. TcOYE also possesses characteristic extra barrel elements, including (i) the N-terminal beta-hairpin (residues 10-19) that closes the bottom of the barrel, (ii) the capping subdomain (105-164), which participates in the formation of the large active-site pocket, (iii) the alpha-helical motif (196-222) related to substrate recognition, and (iv) the inner allpha-helix (336-341) that contributes to FMN binding |
721342 |