1iv4

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Revision as of 18:34, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1iv4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iv4, resolution 1.55Å" /> '''Structure of 2C-Meth...)
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File:1iv4.gif


1iv4, resolution 1.55Å

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Structure of 2C-Methyl-D-erythritol-2,4-cyclodiphosphate Synthase (bound form Substrate)

OverviewOverview

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.

About this StructureAbout this Structure

1IV4 is a Single protein structure of sequence from Thermus thermophilus with MG and C5P as ligands. Active as 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, with EC number 4.6.1.12 Full crystallographic information is available from OCA.

ReferenceReference

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., Kishida H, Wada T, Unzai S, Kuzuyama T, Takagi M, Terada T, Shirouzu M, Yokoyama S, Tame JR, Park SY, Acta Crystallogr D Biol Crystallogr. 2003 Jan;59(Pt 1):23-31. Epub 2002, Dec 19. PMID:12499535

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