Structures of Plasmodium vivax serine hydroxymethyltransferase: implications for ligand-binding specificity and functional control

Chitnumsub, P.; Jaruwat, A.; Riangrungroj, P.; Ittarat, W.; Noytanom, K.; Oonanant, W.; Vanichthanankul, J.; Chuankhayan, P.; Maenpuen, S.; Chen, C.-J.; Chaiyen, P.; Yuthavong, Y.; Leartsakulpanich, U.

doi:10.1107/S1399004714023128

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 3
Binding of (6R)-5FTHF in the ternary PvSHMT–D-Ser–(6R)-5FTHF complex. (a) Interactions between PvSHMT and (6R)-5FTHF, with dashed lines indicating hydrogen-bond distances in Å from residues in protomers A (pink) and B (blue) to the substrates PLP–D-Ser Schiff base (PLD) and (6R)-5FTHF in magenta and a glycerol (GOL) molecule in green. A water molecule (wat; red sphere) forms a bridge between 5FTHF and the protein. (b) Superposition of PvSHMT–D-Ser–(6R)-5FTHF (in blue and pink), ecSHMT–Gly–(6S)-5FTHF (PDB entry 1dfo , white) and rSHMT–PLP–(6S)-triGlu-5FTHF (PDB entry 1ls3 , yellow). Residue labelling is based on the PvSHMT sequence.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 70| Part 12| November 2014| Pages 3177-3186

doi:10.1107/S1399004714023128

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