Table 1.
Amino acid composition of the dimer interfaces formed in PfPGM1 tetrameric state and their sequential conservation
| Interface-1 | Sequence conservation (%) | Interface-2 | Sequence conservation (%) |
|---|---|---|---|
| E35 (SB) [H35] | 20 | R86 (HB) [R86]a | 90 |
| D53 (HB) [D53]a | 100 | K141 (HPB) [A143] | 50 |
| V59 (HPB) [V59]a | 60 | N142 (HPB) [D144] | 10 |
| K61 (HB) [K61]a | 60 | P144 (HPB) [T146] | 40 |
| I64 (HPB) [I64]a | 80 | K145 (HPB) [E147] | 10 |
| C65 (HPB)/(HB) [R65] | 10 | D146 (HB) [D148]a | 20 |
| W68 (HPB) [W68]a | 70 | A147 (HPB) [Q149] | 20 |
| K72 (HPB)/SB [D72] | 30 | P163 (HPB) [P165]a | 100 |
| D75 (HB) [D75]a | 80 | F166 (HPB) [N168] | 20 |
| L77 (HB) [M77] | 30 | D167 (HB) [E169] | 70 |
| H78 (HPB) [W78] | 20 | A170 (HPB) [V172] | 70 |
| V79 (HB) [L79] | 20 | P171 (HPB) [P173]a | 70 |
| K83 (HB) [R83] | 30 | L174 (HPB) [K176] | 30 |
| V139 (HPB) [R141] | 20 | H194 (HPB)/(HB)/SB [H196]a | 50 |
| K141 (HB) [A143] | 50 | N221 (HPB) [N223]a | 50 |
The interface residues were identified using LigPlot software. Sequence conservation (%) represents the positional conservation of respective amino acid in the PfPGM1 protein across the 10 organisms taken into account in this study (Table S1). HB, hydrogen bonding interaction; HPB, hydrophobic interaction SB, salt-bridges interactions are labeled for PfPGM1 protein, as illustrated in Fig. S4, C and D. The corresponding residues of human PGAM located at the same position on the structure are mentioned in square bracket.
a
Shows that the residues are positionally conserved between Plasmodium and human.