1. Volume 2, Issue 5, Pages 361-369 (May 1994)
The three-dimensional structure of N -acetylneuraminate lyase from Escherichia coli 
Tina Izard, Michael C Lawrence, Robyn L Malby, Glenn G Lilley, Peter M Colman 
Structure 
Volume 2, Issue 5, Pages (May 1994)
DOI: /S (00)

2. Figure 1
Cleavage of N-acetylneuraminic acid (Neu5Ac; common name sialic acid) by N-acetylneuraminate lyase.
Structure 1994 2, DOI: ( /S (00) )

3. Figure 2
Stereo Cα trace of the Neu5Ac lyase monomer, viewed down the β -barrel axis from its carboxy-terminal end. Every tenth Cα is labelled. (Figure produced using MOLSCRIPT [10].)
Structure 1994 2, DOI: ( /S (00) )

4. Figure 3
Schematic drawing of the secondary structural elements of Neu5Ac lyase viewed down the β -barrel axis from its carboxy- terminal end. The putative catalytic residue Lys165 (see text) is shown in ball-and-stick representation. (Figure produced using MOLSCRIPT [10].)
Structure 1994 2, DOI: ( /S (00) )

5. Figure 4
Putative active site of Neu5Ac lyase showing the side chains of nine of the residues forming the surface of the pocket. Carbon atoms are white, oxygens black and nitrogen grey. (Figure was produced with MOLSCRIPT [10]).
Structure 1994 2, DOI: ( /S (00) )

6. Figure 5
Backbone ‘worm’ representation of the Neu5Ac lyase tetramer viewed normal to the principal plane. Two protomers are coloured from pink to red and the other two from violet to dark blue with colours growing darker from the amino terminus towards the carboxyl terminus. [Figure produced using HYDRASTER, written by S Watowich and L Gross, based on work by D Bacon and W Anderson (RASTER3D) and R Hubbard (HYDRA).]
Structure 1994 2, DOI: ( /S (00) )

7. Figure 6
Stereoview of the four barrels in the Neu5Ac lyase tetramer. Lys165 in the putative active site is drawn in ball- and-stick representation. Strands a to h have been coloured red, orange, yellow, light green, dark green, light blue, purple and crimson, respectively. The barrel axes are inclined at ∼ 25° to the principal plane of the tetramer and are directed towards a point approximately midway between the centre of the tetramer and the centre of the neighbouring subunit related by the north-south diad in this view. (Figure produced with MOLSCRIPT [10].)
Structure 1994 2, DOI: ( /S (00) )

8. Figure 7
Comparison of the amino acid sequences of Neu5Ac lyase (X ), E. coli dihydrodipicolinate synthase (DHDPS, M ) and the mos A gene product of Rhizobium meliloti (L ). (The numbers in parentheses refer to the entry in the GenBank protein translation database.) Residues identical in the three sequences are marked (∗) whereas residues in the putative active site are marked (+). The alignment was produced by CLUSTAL [23].
Structure 1994 2, DOI: ( /S (00) )

9. Figure 8
Stereoview of the (2F o–F c) electron density map in the vicinity of residue Tyr110. The electron density is contoured at the 1.5σ level. (Figure produced using TURBO FRODO [48].)
Structure 1994 2, DOI: ( /S (00) )