3IWB
T. maritima AdoMetDC in processed form
Summary for 3IWB
| Entry DOI | 10.2210/pdb3iwb/pdb |
| Related | 1TLU 1TMI |
| Descriptor | S-adenosylmethionine decarboxylase (3 entities in total) |
| Functional Keywords | autocatalytic cleavage, decarboxylase, lyase, polyamine biosynthesis, pyruvate, s-adenosyl-l-methionine, schiff base, spermidine biosynthesis, zymogen |
| Biological source | Thermotoga maritima More |
| Total number of polymer chains | 4 |
| Total formula weight | 29615.42 |
| Authors | Bale, S.,Kavita, B.,Ealick, S.E. (deposition date: 2009-09-02, release date: 2010-02-09, Last modification date: 2023-11-15) |
| Primary citation | Bale, S.,Baba, K.,McCloskey, D.E.,Pegg, A.E.,Ealick, S.E. Complexes of Thermotoga maritimaS-adenosylmethionine decarboxylase provide insights into substrate specificity. Acta Crystallogr.,Sect.D, 66:181-189, 2010 Cited by PubMed Abstract: 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'-deoxy-5'-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. PubMed: 20124698DOI: 10.1107/S090744490904877X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.06 Å) |
Structure validation
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