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Structure of a 6-pyruvoyltetrahydropterin synthase homolog from Streptomyces coelicolor.

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.

SUBMITTER: Spoonamore JE

PROVIDER: S-EPMC2564891 | biostudies-literature | 2008 Oct

REPOSITORIES: biostudies-literature

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Structure of a 6-pyruvoyltetrahydropterin synthase homolog from Streptomyces coelicolor.

Spoonamore James E JE Roberts Sue A SA Heroux Annie A Bandarian Vahe V

Acta crystallographica. Section F, Structural biology and crystallization communications 20080930 Pt 10

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-lik ...[more]

PMID: 18931427

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