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Crystallization and preliminary x-ray analysis of tetracenomycin a2 oxygenase: A flavoprotein hydroxylase involved in polyketide biosynthesis

Academic Article
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Overview

authors

  • Beynon, J.
  • Rafanan, E. R., Jr.
  • Shen, Ben
  • Fisher, A. J.

publication date

  • December 2000

journal

  • Acta Crystallographica Section D-Biological Crystallography  Journal

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 A, respectively. The self-rotation function searches in both space groups suggest the monomers assemble into a complex with D(3) symmetry.

subject areas

  • Anthracyclines
  • Antibiotics, Antineoplastic
  • Crystallization
  • Mixed Function Oxygenases
  • Protein Conformation
  • Streptomyces
  • X-Ray Diffraction
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Identity

International Standard Serial Number (ISSN)

  • 0907-4449

Digital Object Identifier (DOI)

  • 10.1107/s0907444900012695

PubMed ID

  • 11092935
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Additional Document Info

start page

  • 1647

end page

  • 1651

volume

  • 56

issue

  • Pt 12

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