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PDBsum entry 1iv2
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structure and catalytic mechanism of 2-C-Methyl-D-Erythritol 2,4-Cyclodiphosphate (mecdp) synthase, An enzyme in the non-Mevalonate pathway of isoprenoid synthesis.
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Authors
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H.Kishida,
T.Wada,
S.Unzai,
T.Kuzuyama,
M.Takagi,
T.Terada,
M.Shirouzu,
S.Yokoyama,
J.R.Tame,
S.Y.Park.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2003,
59,
23-31.
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PubMed id
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Abstract
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Precursors for isoprenoid synthesis are essential in all organisms. These
compounds are synthesized by one of two known routes: the well characterized
mevalonate pathway or a recently discovered non-mevalonate route which is used
in many bacteria and human pathogens. Since the second pathway is both vital and
unlike any found in humans, enzymes catalysing reactions along this synthetic
route are possible drug targets. The structure of one such enzyme from the
thermophilic bacterium Thermus thermophilus has been solved to high resolution
in the presence of substrate and with a substrate analogue. Enzyme
co-crystallized with substrate shows only one product, cytosine monophosphate
(CMP), in the active site. At the high resolution of the refinement (1.6 A) the
positions and coordination of the magnesium ions in the active site are clearly
seen.
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