Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure of a 6-pyruvoyltetrahydropterin synthase homolog from Streptomyces coelicolor.,Spoonamore JE, Roberts SA, Heroux A, Bandarian V Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Oct 1;64(Pt 10):875-9., Epub 2008 Sep 30. PMID:18931427[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Spoonamore JE, Roberts SA, Heroux A, Bandarian V. 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., Epub 2008 Sep 30. PMID:18931427 doi:10.1107/S1744309108027048
