1. Volume 7, Issue 6, Pages 1061-1064 (June 2014)
Structural Basis of Interaction of Bipartite Nuclear Localization Signal from Agrobacterium VirD2 with Rice Importin-α 
Chang Chiung-Wen , Williams Simon J. , Couñago Rafael Miguez , Kobe Bostjan  
Molecular Plant 
Volume 7, Issue 6, Pages (June 2014)
DOI: /mp/ssu014
Copyright © 2014 The Authors. All rights reserved. Terms and Conditions

2. Figure 1
Crystal Structures of the Complexes between rImpα1aΔIBB and the Nucleoplasmin (Npl) and VirD2 NLSs.
(A) Overall structure of the rImpα1aΔIBB (green, cartoon representation):NplNLS (yellow, stick representation) complex. Superimposed is the simulated annealing omit electron density map in the area corresponding to the peptide (contoured at 1.5 σ). Before the simulated annealing run (starting temperature 1000 K), all peptide residues were omitted from the model.
(B) Structures of the NplNLS peptides (in stick representation) after superimposing the structures of rImpα1aΔIBB (yellow) and mImpαΔIBB (magenta; PDB ID 3UL1 (Marfori et al., 2012)) from the respective NplNLS complexes (RMSD = 1.88 Å for 372 Cα atoms).
(C) Schematic diagram of NplNLS bound to rImpα1aΔIBB. The gray horizontal line represents the backbone of the peptide. The blue lines represent the long side chains of the basic residues from the peptide. Residues shown in green and red from rImpα1aΔIBB participate in the hydrogen binding and salt–bridge interactions, respectively.
(D) Overall structure of the rImpα1aΔIBB:VirD2NLS complex, shown as in (A) but with VirD2NLS shown in light blue.
(E) Structures of the VirD2NLS (light blue) and NplNLS (yellow) peptides (in stick representation) after superimposing the structures of rImpα1aΔIBB in the respective complexes (RMSD = Å for 376 Cα atoms).
(F) Schematic diagram of VirD2NLS bound to rImpα1aΔIBB, shown as in (C). The corresponding structural diagram is provided in Supplemental Figure 4.
Molecular Plant 2014 7, DOI: ( /mp/ssu014)
Copyright © 2014 The Authors. All rights reserved. Terms and Conditions