Structure of a 6-pyruvoyltetrahydropterin synthase homolog from Streptomyces coelicolor

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Oct 1;64(Pt 10):875-9. doi: 10.1107/S1744309108027048. Epub 2008 Sep 30.

Abstract

The X-ray crystal structure of the 6-pyruvoyltetrahydropterin synthase (PTPS) homolog from Streptomyces coelicolor, SCO 6650, was solved at 1.5 A 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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Binding Sites
  • Crystallography, X-Ray
  • Models, Molecular
  • Phosphorus-Oxygen Lyases / chemistry*
  • Phosphorus-Oxygen Lyases / metabolism*
  • Protein Conformation
  • Pterins / metabolism
  • Streptomyces coelicolor / enzymology*

Substances

  • Pterins
  • Phosphorus-Oxygen Lyases
  • 6-pyruvoyltetrahydropterin synthase