1u3p

Revision as of 04:42, 21 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1u3p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u3p, resolution 2.85Å" /> '''IspF native'''<br />...)
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IspF native

File:1u3p.jpg


1u3p, resolution 2.85Å

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OverviewOverview

Isoprenoids are biosynthesized from isopentenyl diphosphate and the, isomeric dimethylallyl diphosphate via the mevalonate pathway or a, mevalonate-independent pathway that was identified during the last decade., The non-mevalonate pathway is present in many bacteria, some algae and in, certain protozoa such as the malaria parasite Plasmodium falciparum and in, the plastids of higher plants, but not in mammals and archaea. Therefore, these enzymes have been recognised as promising drug targets. We report, the crystal structure of Escherichia coli 2C-, methyl-d-erythritol-2,4-cyclodiphosphate synthase (IspF), which converts, 4-diphosphocytidyl-2C-methyl-d-erythritol 2-phosphate into, 2C-methyl-d-erythritol 2,4-cyclodiphosphate and CMP in a Mg-dependent, reaction. The protein forms homotrimers that tightly bind one zinc ion per, subunit at the active site, which helps to position the substrate for, direct attack of the 2-phosphate group on the beta-phosphate.

About this StructureAbout this Structure

1U3P is a Single protein structure of sequence from Escherichia coli with ZN as ligand. 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 of 2C-methyl-d-erythritol-2,4-cyclodiphosphate synthase involved in mevalonate-independent biosynthesis of isoprenoids., Steinbacher S, Kaiser J, Wungsintaweekul J, Hecht S, Eisenreich W, Gerhardt S, Bacher A, Rohdich F, J Mol Biol. 2002 Feb 8;316(1):79-88. PMID:11829504

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