Literature DB >> 11173482

Preliminary structural studies of Escherichia coli isopentenyl diphosphate isomerase.

Y Oudjama 1, V Durbecq, G Sainz, B Clantin, C Tricot, V Stalon, V Villeret, L Droogmans.   

Abstract

Escherichia coli isopentenyl diphosphate isomerase, an enzyme catalyzing a key step in isoprenoid biosynthesis, has been produced in selenomethionyl form. The protein was purified and crystallized by the hanging-drop vapour-diffusion method. Crystals display trigonal symmetry, with unit-cell parameters a = b = 71.3, c = 61.7 A, and diffract to 1.45 A resolution.

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Year:  2001        PMID: 11173482     DOI: 10.1107/s0907444900017571

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  3 in total

1.  Monoclinic form of isopentenyl diphosphate isomerase: a case of polymorphism in biomolecular crystals.

Authors:  Jérôme de Ruyck; Yamina Oudjama; Johan Wouters
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2008-03-21

2.  Isopentenyl diphosphate isomerase. Mechanism-based inhibition by diene analogues of isopentenyl diphosphate and dimethylallyl diphosphate.

Authors:  Zheng Wu; Johan Wouters; C Dale Poulter
Journal:  J Am Chem Soc       Date:  2005-12-14       Impact factor: 15.419

3.  Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase.

Authors:  V Durbecq; G Sainz; Y Oudjama; B Clantin; C Bompard-Gilles; C Tricot; J Caillet; V Stalon; L Droogmans; V Villeret
Journal:  EMBO J       Date:  2001-04-02       Impact factor: 11.598

  3 in total

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