 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 2]](cb5045fig2mag.jpg)
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Figure 2
Multiple sequence alignment of PpsR proteins from different organisms. The proteins are listed according to their pairwise sequence identity to PpsR from R. sphaeroides in descending order. The aligned proteins are PpsR from R. sphaeroides (RHOSH, UniProt accession No. Q9S301), PpsR (CrtJ) from Rhodobacter capsulatus (RHOCB, D5ANS9), PpsR from Jannaschia sp. (JANSH, Q28W31), PpsR from Dinoroseobacter shibae (DINSH,A8LQ24), PpsR from Thalassiobium sp. R2A62 (9RHOB, C7DFS5), PpsR (CrtJ) from Rhodospirillum centenum (RHOCS, B6ITX1), PpsR from Rubrivivax gelatinosus (RUBGE, Q8KRL4), PpsR1 from Rhodopseudomonas palustris (RHOPA, Q6N9L3) and Bradyrhizobium sp. (BRASO, Q6A567), and PpsR2 from Rhodopseudomonas palustris (RHOPA, Q6N9K7) and Bradyrhizobium sp. (BRASO, Q8VUB5). The alignment was performed using Jalview (Waterhouse et al., 2009  ) and the MUSCLE algorithm (default settings). The secondary-structure elements are drawn according to protomer A of the PpsRΔHTH structure and a PSIPRED (Buchan et al., 2010) prediction of the secondary-structure elements in the HTH motif. The two cysteine residues Cys251 and Cys424, as well as their corresponding residues in related species, are highlighted in pink and marked with an asterisk. |
![[Figure 2]](cb5045fig2.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
