view article

Figure 3
Solution of the structure of the ternary complex of Escherichia coli dehydrodipicolinate reductase: following the positioning of the central core, the structure was completed using a single N-terminal domain as a search model and the difference Fourier maps generated from the partial solution as the search space. NCS was then used to place two of the remaining three N-terminal domains. The fourth was built into available density following several rounds of refinement of the partial model. The final model revealed that three of the four subunits are in a closed conformation in the ternary complex, with both cofactor and substrate bound to the enzyme, while the fourth subunit is unliganded and in an open conformation.

Journal logoBIOLOGICAL
ISSN: 1399-0047
Follow Acta Cryst. D
Sign up for e-alerts
Follow Acta Cryst. on Twitter
Follow us on facebook
Sign up for RSS feeds