Crystallization and preliminary crystallographic data of SnoaL, a polyketide cyclase in nogalamycin biosynthesis

Acta Crystallogr D Biol Crystallogr. 2004 Jun;60(Pt 6):1118-20. doi: 10.1107/S090744490400705X. Epub 2004 May 21.

Abstract

Nogalonic acid methyl ester cyclase (SnoaL) catalyzes the last ring-closure step in the biosynthesis of the polyketide antibiotic nogalamycin. Crystals of a complex of SnoaL with the substrate nogalonic acid methyl ester have been obtained using PEG 4000 as precipitant. The crystals are orthorhombic, space group I222, with unit-cell parameters a = 69.1, b = 72.0, c = 65.4 angstroms. They diffract to 1.35 angstroms resolution using synchrotron radiation. A Matthews coefficient of 2.0 angstroms3 Da(-1) suggests one subunit in the asymmetric unit. Diffraction data for an isomorphous uranium derivative were collected and a difference Patterson map showed strong peaks which allowed determination of the position of the uranium ions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Antibiotics, Antineoplastic / chemistry
  • Bacterial Proteins
  • Crystallography, X-Ray / methods*
  • Escherichia coli / metabolism
  • Hydrogen-Ion Concentration
  • Ions
  • Isomerases / chemistry*
  • Models, Chemical
  • Molecular Sequence Data
  • Nogalamycin / biosynthesis*
  • Polyethylene Glycols / chemistry
  • Streptomyces / enzymology*
  • Substrate Specificity
  • Synchrotrons
  • Uranium / chemistry
  • Uranium / metabolism

Substances

  • Antibiotics, Antineoplastic
  • Bacterial Proteins
  • Ions
  • Polyethylene Glycols
  • Uranium
  • Isomerases
  • nogalonic acid methyl ester cyclase
  • Nogalamycin