 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 4]](hm5052fig4mag.jpg)
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Figure 4
Active-site superpositions. (a) The E109Q (blue) mutant protein superimposed on the wild-type (gray) PvlArgDC. No significant conformational changes were observed. (b) Superposition of N47A (blue) with the unprocessed S53A mutant protein (gray). Although both mutant proteins show no processing in this chain, there is a shift in the Ile54 position in the N47A mutant, most likely owing to loss of hydrogen bonding. (c) Comparison of three protomers from one asymmetric unit of the N47A mutant protein. This mutation resulted in increased flexibility in the key residues involved in the autoprocessing reaction. In all panels residues labelled with a prime are from a second protomer. |
![[Figure 4]](hm5052fig4.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
