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PDBsum entry 3iwc
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References listed in PDB file
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Key reference
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Title
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Complexes of thermotoga maritimas-Adenosylmethionine decarboxylase provide insights into substrate specificity.
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Authors
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S.Bale,
K.Baba,
D.E.Mccloskey,
A.E.Pegg,
S.E.Ealick.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2010,
66,
181-189.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 4.
Figure 4 Schematic view of the interactions of MeAdoMet in the
active site of TmAdoMetDC.
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Figure 7.
Figure 7 Stereoview of a comparison of the active sites of
TmAdoMetDC (C atoms colored green) and hAdoMetDC (C atoms
colored cyan) with MeAdoMet bound. Hydrogen bonds are omitted
for clarity.
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2010,
66,
181-189)
copyright 2010.
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