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Figure 1
Crystal structures for the five proteins of this study represented as ribbons with colour-coded secondary structures (helices: cyan; β-strands: magenta; other: orange) with a semi-transparent surface (orange) overlay. The PDB entry, resolution and molecular mass from chemical composition for each protein is: RNase A, 7rsa, 1.26 Å, 13.690 kDa; lysozyme, 2vb1, 0.65 Å, 14.313 kDa; xylanase, 2dfc, 1.19 Å, 20.825 kDa; urate oxidase tetramer, 3l8w, 1.00 Å, 136.603 kDa; xylose isomerase tetramer, 1mnz, 0.99 Å, 172.910 kDa, respectively. The urate oxidase tetramer structure includes an added C-terminal SLKSKL missing from the crystal structure, whereas the xylose isomerase includes a missing N-terminal me­thio­nine. Amino acids 47–48, 80–81 and 102–104 in RNase A, shown as orange spheres, form the hinge at the base of the V shape of the three β-strands that facilitates subtle domain dynamics required for RNase A activity.

IUCrJ
Volume 11| Part 5| September 2024|
ISSN: 2052-2525
https://doi.org/10.1107/S205225252400486X