Structure of a 6-pyruvoyltetrahydropterin synthase homolog from Streptomyces coelicolor

James E. Spoonamore, Sue A. Roberts, Annie Heroux, Vahe Bandarian

Research output: Contribution to journalArticle

2 Scopus citations

Abstract

The X-ray crystal structure of the 6-pyruvoyltetrahydropterin synthase (PTPS) homolog from Streptomyces coelicolor, SCO 6650, was solved at 1.5 Å resolution. SCO 6650 forms a hexameric T-fold that closely resembles other PTPS proteins. The biological activity of SCO 6650 is unknown, but it lacks both a required active-site zinc metal ion and the essential catalytic triad and does not catalyze the PTPS reaction. However, SCO 6650 maintains active-site residues consistent with binding a pterin-like substrate.

Original languageEnglish (US)
Pages (from-to)875-879
Number of pages5
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume64
Issue number10
DOIs
StatePublished - Oct 17 2008

Keywords

  • 6-pyruvoyltetrahydropterin synthase homolog
  • SCO 6650
  • Streptomyces coelicolor

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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