view article
Figure 3
Topology of S. meliloti AFR. (a) Arrangement of the secondary-structure elements within one molecule. The figure was generated using PDBsum (Laskowski, 2009BB27). (b) Ribbon representation of AFR and the putative dimeric assembly of the active enzyme. The secondary-structure elements of the molecule within the crystallo­graphic asymmetric unit are coloured cyan (α-helices), red (β-sheets) and magenta (loops). The bound cofactor NADP(H) is displayed in ball-and-stick representation. The molecule in green represents the (x, −y, −z) symmetry mate. Intermolecular contacts are formed between the two extended β-sheets of the C-­terminal domain to build the stable dimer as observed in solution.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 69| Part 8| July 2013| Pages 844-849
doi:10.1107/S1744309113019490
Follow Acta Cryst. F
Sign up for e-alerts
E-alerts
Follow Acta Cryst. on Twitter
Twitter
Follow us on facebook
Facebook
Sign up for RSS feeds
RSS