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Figure 2
(a) A sequence alignment based on the crystal structures of PGABN and SlCE4 (PDB entry 2cc0 ). Conserved residues are shown in white on a red background. Red triangles show residues that coordinate the active-site zinc ion and blue triangles show nearby residues involved in catalysis. The residue numbering refers to PGABN. The first β-strand of PGABN (residues 48–55) matches the last strand of SlCE4, the sequence of which has been shifted from the C-terminus to the N-terminus in this alignment. His55 of PGABN matches His155 of SlCE4. The figure was produced by ESPript (Gouet et al., 1999 ). (b) Overlay of the Cα traces of the PgaB N-domain and SlCE4 (PDB entry 2cc0
), showing the helices and strands of both structures, but not coil. Alignment of the models was carried out with SSM (Krissinel & Henrick, 2004 ). Each structure is coloured from blue to red (N-terminus to C-terminus) as in (a), but circular permutation of the sequences leads to a marked difference in colouring, despite the close structural similarity. His55 of PGABN lies close to the active site, overlapping His155 of SlCE4, which is a conserved histidine in the CE4 family. |


journal menu![[Figure 2]](mh5070fig2.jpg)




