1. Volume 4, Issue 6, Pages 715-724 (June 1996)
Crystal structure of transaldolase B from Escherichia coli suggests a circular permutation of the α/β barrel within the class I aldolase family 
Jia Jia, Weijun Huang, Ulrich Schö rken, Hermann Sahm, Georg A Sprenger, Ylva Lindqvist, Gunter Schneider 
Structure 
Volume 4, Issue 6, Pages (June 1996)
DOI: /S (96)

2. Figure 1
Reactions catalyzed by (a) transaldolase and (b) fructose-1,6-bisphosphate aldolase.
Structure 1996 4, DOI: ( /S (96) )

3. Figure 1
Reactions catalyzed by (a) transaldolase and (b) fructose-1,6-bisphosphate aldolase.
Structure 1996 4, DOI: ( /S (96) )

4. Figure 2
Stereodiagram showing part of the final 2Fo−Fc electron-density map for transaldolase, contoured at 1.0σ.
Structure 1996 4, DOI: ( /S (96) )

5. Figure 3
Ramachandran plot for the refined model of transaldolase. Triangles represent glycine and squares represent non-glycine residues.
Structure 1996 4, DOI: ( /S (96) )

6. Figure 4
Schematic view of the subunit of transaldolase from E. coli. The β strands are coloured in green, the helices pink and the connecting loops yellow. Conserved polar amino acids at the active site are included as ball-and-stick models. The figure was generated using the program MOLSCRIPT [36].
Structure 1996 4, DOI: ( /S (96) )

7. Figure 5
Stereoview of the Cα trace of a subunit of transaldolase. Every tenth residue is indicated.
Structure 1996 4, DOI: ( /S (96) )

8. Figure 6
Assignment of secondary structure elements of transaldolase and sequence alignment of transaldolase with the amino-acid sequence of human muscle aldolase based on the comparison of their 3D structure. Secondary structure assignments were made with the program DSSP [37]. The first line shows secondary structure elements of transaldolase; second line, amino-acid sequence of transaldolase from E. coli [3]; third line, sequence alignment of human muscle aldolase, using the structural superposition in which the strands carrying the Schiff-base-forming lysine were aligned (alignment β4→β6); fourth line, sequence alignment of human muscle aldolase, using the structural alignment in which the strands were superposed in order of appearance (alignment β1→β1). Conserved residues in both enzymes are shaded in grey, and the Schiff-base-forming lysine residues are enclosed in rectangles.
Structure 1996 4, DOI: ( /S (96) )

9. Figure 7
Active-site peptide of transaldolase from Candida utilis, carrying the Schiff-base-forming lysine residue, and alignment of homologous regions in the amino-acid sequences of transaldolases. Conserved residues are indicated by bold letters [3,6,7,11].
Structure 1996 4, DOI: ( /S (96) )

10. Figure 8
Superposition of a single subunit from transaldolase (red) and aldolase (blue). The superposition is based on alignment β4→β6 (for details see text).
Structure 1996 4, DOI: ( /S (96) )