Crystal structure of a putative protein-L-isoaspartate O-methyltransferase beta-aspartate methyltransferase (PCMT) from Plasmodium falciparum in complex with S-adenosyl-L-homocysteine

Protein-L-isoaspartate O-methyltransferase beta-aspartate methyltransferase

GNNMYKLSENNHKSLLENLKRRGIIDDDDVYNTMLQVDRGKYIKEIPYIDTPVYISHGVTISAPHMHALSLKRLINVLKP
GSRAIDVGSGSGYLTVCMAIKMNVLENKNSYVIGLERVKDLVNFSLENIKRDKPELLKIDNFKIIHKNIYQVNEEEKKEL
GLFDAIHVGASASELPEILVDLLAENGKLIIPIEEDYTQVLYEITKKNGKIIKDRLFDVCFVSLKKN

25% PEG 3350, 0.2 M (NH4)2SO4, 0.1 M Hepes pH 7.2, 2 mM SAH, VAPOR DIFFUSION, SITTING DROP, temperature 298K

BIOMOLECULE: 1, 2
THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
WHICH CONSISTS OF 2 CHAIN(S). AUTHORS STATE THAT THE
BIOLOGICAL UNIT OF THIS PROTEIN IS A MONOMER.
SEE REMARK 350 FOR INFORMATION ON GENERATING THE
BIOLOGICAL MOLECULE(S).

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

methyltransferase, protein repair, isoaspartyl formation, P. falciparum, Structural Genomics Consortium, SGC, TRANSFERASE

NNMYKLSENNHKSLLENLKRRGIIDDDDVYNTMLQVDRGKYIKEIPYIDTPVYISHGVTISAPHMHALSLKRLINVLKPG
SRAIDVGSGSGYLTVCMAIKMNVLENKNSYVIGLERVKDLVNFSLENIKRDKPELLKIDNFKIIHKNIYQVNEEEKKELG
LFDAIHVGASASELPEILVDLLAENGKLIIPIEEDYTQVLYEITKKNGKIIKDRLFDVCFVSLKKN