Crystallization and preliminary X-ray studies on the putative dTDP sugar epimerase NovW from the novobiocin biosynthetic cluster of Streptomyces spheroides

Piotr Jakimowicz, Caren L Meyers, Christopher T. Walsh, Mark J. Buttner, David M. Lawson

Research output: Contribution to journalArticle

Abstract

Crystals of recombinant NovW (subunit MW = 22 289 Da), a putative dTDP sugar epimerase from Streptomyces spheroides, were grown by vapour diffusion. The protein crystallizes in space group P43212, with unit-cell parameters a = b = 59.20, c = 109.23 Å. Native data to a resolution of 2.0 Å were collected from a single crystal at 100 K on a rotating-anode X-ray generator. Preliminary analysis of these data indicated that the asymmetric unit corresponded to a monomer, whilst dynamic light scattering (DLS) suggested that NovW was a dimer in solution. NovW is involved in the biosynthesis of the aminocoumarin antibiotic novobiocin, which targets the bacterial enzyme DNA gyrase, and represents the first enzyme to be crystallized from this biosynthetic pathway.

Original languageEnglish (US)
Pages (from-to)1507-1509
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume59
Issue number8
DOIs
StatePublished - Aug 1 2003
Externally publishedYes

Fingerprint

Novobiocin
Racemases and Epimerases
Streptomyces
sugars
Crystallization
Sugars
enzymes
Aminocoumarins
X-Rays
crystallization
DNA Gyrase
X rays
Bacterial DNA
biosynthesis
antibiotics
Biosynthesis
Biosynthetic Pathways
Dynamic light scattering
Enzymes
Dimers

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics
  • Condensed Matter Physics
  • Structural Biology

Cite this

Crystallization and preliminary X-ray studies on the putative dTDP sugar epimerase NovW from the novobiocin biosynthetic cluster of Streptomyces spheroides. / Jakimowicz, Piotr; Meyers, Caren L; Walsh, Christopher T.; Buttner, Mark J.; Lawson, David M.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 59, No. 8, 01.08.2003, p. 1507-1509.

Research output: Contribution to journalArticle

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