Crystal structure of CymD prenyltransferase complexed with L-tryptophan and DMSPP

DMASPP; DMAPP; DMADP; Dimethylallyl pyrophosphate; dimethylallyl diphosphate; isoprenyl pyrophosphate

Structural Basis of Tryptophan Reverse N-Prenylation Catalyzed by CymD.

SNATEELTTVRDACARTLENTARTLHLGASGTEFVAAFRAMTDHWGAARPHDLPLSDVSPDGSPVEYAVDLGGLAPALQF
AMEPLTAGVPARDPLAARAIMPLLAGRYGADATRWSALADRLLPDDAHGPHVSMYGAEVRAGAPIRFKAWFYLNVTGPDG
AFNLLYSALERMGTTHLWPVVQAHVHRAGEDVPFLLSLDLSDDPAARVKVYFRHFAADVEEVAAVLKAYPGFEPGEVRAF
CKVMMGGRRRFSDQPAVTCVSLLDAQTFDRTAATLYVPLWTYAEHDGEVRQRVHRTLAAWPEALYRYDSVLAGIAHRGLD
AGTGIHNYISWQPGRTRPRMKVYLSPEMHDVTPPPLGVSQQHHLSGQTTARGRTE

National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)

Author used SWISS-MODEL server to generate a phasing model based on the protein sequence. SWISS-MODEL produced a phasing model based on PDB Entry 5JXM. Author used the polyALA version of the model for phasing.

prenyltransferase, tryptophan, indole, biosynthesis, TRANSFERASE

TEELTTVRDACARTLENTARTLHLGASGTEFVAAFRAMTDHWGAARPHDLPLSDVSPDGSPVEYAVDLGGLAPALQFAME
PLTAGVPARDPLAARAIMPLLAGRYGADATRWSALADRLLPDDAHGPHVSMYGAEVRAGAPIRFKAWFYLNVTGPDGAFN
LLYSALERMGTTHLWPVVQAHVHRAGEDVPFLLSLDLSDDPAARVKVYFRHFAADVEEVAAVLKAYPGFEPGEVRAFCKV
MMGGRRRFSDQPAVTCVSLLDAQTFDRTAATLYVPLWTYAEHDGEVRQRVHRTLAAWPEALYRYDSVLAGIAHRGLDAGT
GIHNYISWQPGRTRPRMKVYLSPEMHDVTPPPLGVSQQHHLSGQTTARGRTE