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PDBsum entry 2p3v
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the tetrameric inositol 1-Phosphate phosphatase (tm1415) from the hyperthermophile, Thermotoga maritima.
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Authors
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K.A.Stieglitz,
M.F.Roberts,
W.Li,
B.Stec.
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Ref.
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Febs J, 2007,
274,
2461-2469.
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PubMed id
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Abstract
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The structure of the first tetrameric inositol monophosphatase (IMPase) has been
solved. This enzyme, from the eubacterium Thermotoga maritima, similarly to its
archaeal homologs exhibits dual specificity with both IMPase and
fructose-1,6-bisphosphatase activities. The tetrameric structure of this
unregulated enzyme is similar, in its quaternary assembly, to the allosterically
regulated tetramer of fructose-1,6-bisphosphatase. The individual dimers are
similar to the human IMPase. Additionally, the structures of two crystal forms
of IMPase show significant differences. In the first crystal form, the
tetrameric structure is symmetrical, with the active site loop in each subunit
folded into a beta-hairpin conformation. The second form is asymmetrical and
shows an unusual structural change. Two of the subunits have the active site
loop folded into a beta-hairpin structure, whereas in the remaining two subunits
the same loop adopts an alpha-helical conformation.
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