EC Number   |
|---|
    2.3.3.21 | C-terminal regulatory domain of CMS (CMSC) in complex with isoleucine, by hanging-drop vapour diffusion method. Crystals of CMSC belong to space group C222 (type I) with unit cell parameters a = 62.6 A, b = 98.4 A and c = 40.1 A, refined to 2.5 A resolution. Type II crystals of CMSC grown at room temperature belong to space group C2 with unit cell parameters a = 61.3 A, b = 97.9 A, c = 40.0 A and beta = 91.4, refined to 2.0 A resolution. Type III crystals of CMSC grown at 4°C belong to space group C222 with unit cell parameters a = 108.2 A, b = 118.6 A and c = 63.6 A, refined to 2.7 A resolution. CMSC consists of six beta-strands forming two anti-parallel beta-sheets and two alpha-helices and assumes a betaalphabeta three-layer sandwich structure. The inhibitor isoleucine is bound in a pocket at the dimer interface and has both hydrophobic and hydrogen-bonding interactions with several conserved residues of both subunits |
| 2.3.3.21 | full-length LiCMS protein is used for the crystallization experiments, which are performed at room temperature (20°C) using the hanging-drop vapour-diffusion method. Crystal structures of the catalytic domain of LiCMS and its complexes with substrates |
| 2.3.3.21 | hanging-drop vapor diffusion, in 20 mM Tris-HCl, pH 8.4 with 50 mM NaCl |
| 2.3.3.21 | the crystal structures of LiCMSN, the N-terminal catalytic domain, in complex with malonate at 2.0 A resolution, in complex with pyruvate at 2.6 A resolution, and in complex with pyruvate and acetyl-CoA at 2.5 A are reported |
| 2.3.3.21 | the crystal structures of the catalytic domains of LiCMS and its complexes with substrates are solved |
