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  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., et al. (2002). Structure of 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase involved in mevalonate-independent biosynthesis of isoprenoids. Journal of Molecular Biology, 316(1), 79-88.

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Genre: Zeitschriftenartikel
Alternativer Titel : J. Mol. Biol.

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 Urheber:
Steinbacher, S.1, Autor           
Kaiser, J., Autor
Wungsintaweekul, J., Autor
Hecht, S., Autor
Eisenreich, W., Autor
Gerhardt, S.1, Autor           
Bacher, A., Autor
Rohdich, F., Autor
Affiliations:
1Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565155              

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Schlagwörter: antibiotics; crystal structure; isoprenoid biosynthesis; malaria; non-mevalonate pathway
 Zusammenfassung: 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. (C) 2002 Elsevier Science Ltd.

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Sprache(n): eng - English
 Datum: 2002-02-08
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 39111
ISI: 000174025900007
 Art des Abschluß: -

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Titel: Journal of Molecular Biology
  Alternativer Titel : J. Mol. Biol.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 316 (1) Artikelnummer: - Start- / Endseite: 79 - 88 Identifikator: ISSN: 0022-2836