Crystal structures of the 3C proteases from Coxsackievirus B3 and B4

Jiang, H.; Lin, C.; Chang, J.; Zou, X.; Zhang, J.; Li, J.

doi:10.1107/S2053230X24006915

Figure 2
Crystal structure of the 3C protease from CVB4. (a) Overall structure of the CVB4 3C protease. The two molecules (molecule A and molecule B) in the asymmetric unit of the CVB4 3C protease structure are shown in cartoon representation. Molecule B (cyan) is packed against the surface of molecule A (green). (b) A magnified view showing detailed crystal-packing interactions. The residues involved in crystal packing are shown as sticks. Hydrogen-bonding interactions are indicated as black dashed lines. W represents the water molecule that mediates hydrogen-bonding interactions. (c) Comparison of molecule A and molecule B in the CVB4 3C protease structure. The catalytic residues (His40, Glu71 and Cys147) are shown as sticks. (d) Overall structure of molecule A. The structure is colored from blue at the N-terminus to green at the C-terminus. Four α-helices in two domains (I and II) are marked αA–αD. A total of 16 β-strands are labeled (βaI–βgI in domain I and βaII–βgII in domain II) according to their occurrence along the primary structure. (e) Catalytic triad and RNA-binding sites of the CVB4 3C protease. The 2F_o − F_c electron densities for the catalytic residues are contoured at 1σ. The RNA-binding motifs, KFRDI and TGK, are colored magenta.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 80| Part 8| August 2024| Pages 183-190

https://doi.org/10.1107/S2053230X24006915

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