 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](nw5126fig1mag.jpg)
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Figure 1
Crystal structure of the 3C protease from CVB3. (a) Overall structure of the CVB3 3C protease. The structure is colored from blue at the N-terminus to red at the C-terminus. The α-helices in the two domains (I and II) are labeled αA–αD. The β-strands are labeled βaI–βgI in domain I and βaII–βgII in domain II according to their occurrence along the primary structure. (b) Catalytic triad and RNA-binding sites of the CVB3 3C protease. The 2Fo − Fc electron densities for the catalytic residues (His40, Glu71 and Cys147) are contoured at 1σ. The RNA-binding motifs, KFRDI and TGK, are colored green. (c) Comparison of structures of the CVB3 3C protease. The structure solved in this study is colored magenta. The structures solved previously, named form I (PDB entry 2zty) and form II (PDB entry 2ztz), are colored cyan and orange, respectively. The loop consisting of residues 143–146 (the 143–146 loop) is indicated by a green arrow. (d) An enlarged view of the comparison of catalytic residues. The catalytic residues are shown as sticks. Electron density for Cys147 is missing in our structure. |
![[Figure 1]](nw5126fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
