 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 3]](dp5074fig3mag.jpg)
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Figure 3
(a) Alignment via Chimera MatchMaker of PfAldolase (PDB entry 1a5c , chain A), PfAldolase bound to TRAP (PDB entry 2pc4 , chain D) and TgAldolase (PDB entry 4tu1 , chains A and D) represented as cartoons. The TRAP peptide shown in stick representation with two coordinating waters is present in the active site, which doubles as the adhesin tail binding pocket. A box highlights the dual conformation of the Met285–Ala296 loop in the TgAldolase chain A and D and PfAldolase structures. (b) Sequence conservation between TgAldolase and PfAldolase mapped on a surface representation of TgAldolase, with magenta indicating identical residues and cyan representing differences. (c) Surface representation of TgAldolase chain A colored according to residue r.m.s.d. (Å) from the reference structure PfAldolase (PDB entry 1a5c , chain A). (d) Three-panel enlargement of the adhesin-binding site of (left) TRAP bound to PfAldolase (PDB entry 2pc4 ), (middle) apo PfAldolase (PDB entry 1a5c ) and (right) TgAldolase chain A, with residues important for TRAP binding highlighted as sticks. |
![[Figure 3]](dp5074fig3.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
