Steve Ealick's Research Group
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Steve Ealick's Research Group |
Thermatoga maritima S-Adenosylmethionine Decarboxylase
PDB files:
1TLU, wild type TMAdoMetDC
1TMI, S63A mutant of TMAdoMetDC
Description:
Solution of the structure of Thermatoga maritima S-adenosylmethionine decarboxylase (TmAdoMetDC) continues our work on enzymes of the polyamine biosynthetic pathway. AdoMetDC is a critical regulatory enzyme in the polyamine synthetic pathway and is a target of drug design.The TmAdoMetDC structure provides striking evidence of an ancient gene duplication event resulting in the class 2 AdoMetDC enzymes (which incudes human and potato AdoMetDC's).
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The architecture of each protomer (designated A and B) is a two-layer αβ-sandwich with an anti-parallel β-sheet flanked by two α-helices and a short 310-helix.
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Click the image to enlarge. |
| The active form of TmAdoMetDC is an (αβ)2 dimer. Each protomer contains one active site that occurs at the dimer interface and also requires residues from the adjacent protomer.This dimer has a striking similarity to the monomer from potato AdoMetDC. |
Click the image to enlarge. |
| A hydrogen bonding network connects the two active sites in the dimer interface of the TmAdoMetDC. |
Click the image to enlarge. |
Reference:
Toms AV, Kinsland C, McCloskey DE, Pegg AE and Ealick SE. Evolutionary Links as Revealed by the Structure of Thermotoga maritima S-adenosylmethionine Decarboxylase. J. Biol. Chem. 279:33837-33846 (2004).
