Crystallization and preliminary X-ray analysis of tetracenomycin A2 oxygenase: A flavoprotein hydroxylase involved in polyketide biosynthesis

J. Beynon, Jr Rafanan E.R., B. Shen, Andrew J Fisher

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

The tcm operon in Streptomyces glaucescens encodes a group of enzymes involved in the synthesis of the polyketide tetracenomycin (Tcm) C that exhibits both antitumor and antibiotic activities. Here, the crystallization and preliminary data characterization of the tcmG gene product, Tcm A2 oxygenase, which catalyzes the triple hydroxylation of Tcm A2 to form Tcm C, are reported. Tcm A2 oxygenase crystallizes in two different space groups, both with six monomers per asymmetric unit, resulting in large unit-cell parameters. Synchrotron data have been collected from both the hexagonal and tetragonal crystal forms to 4.5 and 4.2 Å, respectively. The self-rotation function searches in both space groups suggest the monomers assemble into a complex with D3 symmetry.

Original languageEnglish (US)
Pages (from-to)1647-1651
Number of pages5
JournalActa Crystallographica Section D: Biological Crystallography
Volume56
Issue number12
DOIs
StatePublished - 2000

Fingerprint

Polyketides
Flavoproteins
biosynthesis
Biosynthesis
X ray analysis
Mixed Function Oxygenases
Crystallization
Monomers
X-Rays
crystallization
Hydroxylation
Synchrotrons
Streptomyces
Operon
monomers
x rays
antibiotics
Genes
Anti-Bacterial Agents
genes

ASJC Scopus subject areas

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

Cite this

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title = "Crystallization and preliminary X-ray analysis of tetracenomycin A2 oxygenase: A flavoprotein hydroxylase involved in polyketide biosynthesis",
abstract = "The tcm operon in Streptomyces glaucescens encodes a group of enzymes involved in the synthesis of the polyketide tetracenomycin (Tcm) C that exhibits both antitumor and antibiotic activities. Here, the crystallization and preliminary data characterization of the tcmG gene product, Tcm A2 oxygenase, which catalyzes the triple hydroxylation of Tcm A2 to form Tcm C, are reported. Tcm A2 oxygenase crystallizes in two different space groups, both with six monomers per asymmetric unit, resulting in large unit-cell parameters. Synchrotron data have been collected from both the hexagonal and tetragonal crystal forms to 4.5 and 4.2 {\AA}, respectively. The self-rotation function searches in both space groups suggest the monomers assemble into a complex with D3 symmetry.",
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AU - Rafanan E.R., Jr

AU - Shen, B.

AU - Fisher, Andrew J

PY - 2000

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