view article
Figure 4
The surface potentials of the three related proteins. (a) P. horikoshii RNA ligase, (b) T. thermophilus RNA ligase, (c) CPDase. The two histidines modelled as alternate conformations in T. thermophilus RNA ligase were reduced to the conformation most closely matching the equivalent residues in the P. horikoshii RNA ligase. The orientation of the two RNA ligases is identical and placed to enhance the positive patch of the T. thermophilus RNA ligase. The orientation of the CPDase was chosen to match the active-site histidines of the RNA-ligase structures.

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
Volume 61| Part 9| September 2005| Pages 1207-1212
https://doi.org/10.1107/S0907444905017841
Follow Acta Cryst. D
Sign up for e-alerts
E-alerts
Follow Acta Cryst. on Twitter
Twitter
Follow us on facebook
Facebook
Sign up for RSS feeds
RSS