Crystal structure of a putative transcriptional regulator SCO0520 from Streptomyces coelicolor A3(2) reveals an unusual dimer among TetR family proteins

Ekaterina V. Filippova, Maksymilian Chruszcz, Marcin Cymborowski, Jun Gu, Alexei Savchenko, Aled Edwards, Wladek Minor*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

Abstract

A structure of the apo-form of the putative transcriptional regulator SCO0520 from Streptomyces coelicolor A3(2) was determined at 1.8 Å resolution. SCO0520 belongs to the TetR family of regulators. In the crystal lattice, the asymmetric unit contains two monomers that form an shaped dimer. The distance between the two DNA-recognition domains is much longer than the corresponding distances in the known structures of other TetR family proteins. In addition, the subunits in the dimer have different conformational states, resulting in different relative positions of the DNA-binding and regulatory domains. Similar conformational modifications are observed in other TetR regulators and result from ligand binding. These studies provide information about the flexibility of SCO0520 molecule and its putative biological function.

Original languageEnglish (US)
Pages (from-to)149-157
Number of pages9
JournalJournal of Structural and Functional Genomics
Volume12
Issue number3
DOIs
StatePublished - Sep 2011

Keywords

  • Helix-turn-helix DNA-binding motif
  • Structural genomics
  • TetR transcriptional regulator
  • X-ray crystal structure

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics

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