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Structure paper

TitleMode of binding of methyl acceptor substrates to the adrenaline-synthesizing enzyme phenylethanolamine N-methyltransferase: implications for catalysis
Journal, issue, pagesBiochemistry, Vol. 44, Page 16875-16885, Year 2005
Publish dateAug 11, 2005 (structure data deposition date)
AuthorsGee, C.L. / Tyndall, J.D.A. / Grunewald, G.L. / Wu, Q. / McLeish, M.J. / Martin, J.L.
External linksBiochemistry / PubMed:16363801
MethodsX-ray diffraction
Resolution2.2 - 2.5 Å
Structure data

PDB-2an3:
Structure of PNMT with S-adenosyl-L-homocysteine and the semi-rigid analogue acceptor substrate cis-(1R,2S)-2-amino-1-tetralol.
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-2an4:
Structure of PNMT complexed with S-adenosyl-L-homocysteine and the acceptor substrate octopamine
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-2an5:
Structure of human PNMT complexed with S-adenosyl-homocysteine and an inhibitor, trans-(1S,2S)-2-amino-1-tetralol
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

ChemComp-CTL:
CIS-(1R,2S)-2-AMINO-1,2,3,4-TETRAHYDRONAPHTHALEN-1-OL

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

ChemComp-OTR:
4-(2R-AMINO-1-HYDROXYETHYL)PHENOL

ChemComp-TTL:
TRANS-(1S,2S)-2-AMINO-1,2,3,4-TETRAHYDRONAPHTHALEN-1-OL

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / methyltransferase / substrate structure / S-adenosyl-L-methionine / adrenaline synthesis / inhibitor structure

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