Complexes of Thermotoga maritima S-adenosylmethionine decarboxylase provide insights into substrate specificity

Journal Article · Fri Jun 25 04:00:00 EDT 2010 · Acta Crystallogr. D

DOI:https://doi.org/10.1107/S090744490904877X· OSTI ID:1002475

Bale, Shridhar; Baba, Kavita; McCloskey, Diane E; Pegg, Anthony E; Ealick, Steven E

The polyamines putrescine, spermidine and spermine are ubiquitous aliphatic cations and are essential for cellular growth and differentiation. S-Adenosylmethionine decarboxylase (AdoMetDC) is a critical pyruvoyl-dependent enzyme in the polyamine-biosynthetic pathway. The crystal structures of AdoMetDC from humans and plants and of the AdoMetDC proenzyme from Thermotoga maritima have been obtained previously. Here, the crystal structures of activated T. maritima AdoMetDC (TmAdoMetDC) and of its complexes with S-adenosylmethionine methyl ester and 5{prime}-deoxy-5{prime}-dimethylthioadenosine are reported. The results demonstrate for the first time that TmAdoMetDC autoprocesses without the need for additional factors and that the enzyme contains two complete active sites, both of which use residues from both chains of the homodimer. The complexes provide insights into the substrate specificity and ligand binding of AdoMetDC in prokaryotes. The conservation of the ligand-binding mode and the active-site residues between human and T. maritima AdoMetDC provides insight into the evolution of AdoMetDC.

• Research Organization: Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
• Sponsoring Organization: USDOE
• OSTI ID: 1002475
• Journal Information: Acta Crystallogr. D, Journal Name: Acta Crystallogr. D Journal Issue: (2) ; 02, 2010 Vol. 66
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

36 MATERIALS SCIENCE
CATIONS
CHAINS
CRYSTAL STRUCTURE
DECARBOXYLASES
ENZYMES
ESTERS
PUTRESCINE
RESIDUES
SPECIFICITY
SPERMIDINE
SPERMINE
SUBSTRATES