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 language | English (US) |
|---|---|
| Pages (from-to) | 875-879 |
| Number of pages | 5 |
| Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
| Volume | 64 |
| Issue number | 10 |
| DOIs | |
| State | Published - 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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SCO6650, a 6-pyruvoyltetrahydropterin synthase homolog from Streptomyces coelicolor
Spoonamore, J. E. (Contributor), Roberts, S. A. (Contributor), Heroux, A. (Contributor) & Bandarian, V. (Contributor), Protein Data Bank (PDB), Oct 21 2008
DOI: 10.2210/pdb3D7J/pdb, https://www.wwpdb.org/pdb?id=pdb_00003d7j
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