 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 1]](dz5336fig1mag.jpg)
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Figure 1
Comparison of Vap sequences. (a) Amino-acid residue sequence alignment of the mature Vap proteins encoded by the plasmids pVAPA1037 (Takai et al., 2000  ) and pVAPB1593 (Letek et al., 2008). Invariant residues in the alignment are shown in white on a red background; conserved residues are in blue boxes. The secondary structure for VapD is indicated above the alignment. Black triangles highlight four conserved amino-acid residues involved in the amide cluster referred to in the text. (b) Alignment of the sequences of R. equi Vap homologues from diverse species. The aligned sequences with their UniProt accession codes are VapD (ReVapD; B4F3C5) and VapA (ReVapA; B4F3C2) from R. equi and homologues from Xenorhabdus bovienii (Xbovi; D3V6D4), Halomonas titaniciae BH1 (Htita; L9UBC3), Lacinutrix sp. strain 5H374 (Lacin; F6GHM2), Escherichia coli H263 (Ecoli; 9VNI1) and Clostridium sp. DL-VIII (Clost; G7LYQ8). For this comparison the 30-residue signal peptide of VapD is retained, so the numbering is different to that used in (a). |
![[Figure 1]](dz5336fig1.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
