Structure of a 6-pyruvoyltetrahydropterin synthase homolog from Streptomyces coelicolor

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

doi:10.1107/S1744309108027048

Structure of a 6-pyruvoyltetrahydropterin synthase homolog from Streptomyces coelicolor

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

Chemistry and Biochemistry

Research output: Contribution to journal › Article › peer-review

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 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	https://doi.org/10.1107/S1744309108027048
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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10.1107/S1744309108027048

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title = "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 {\AA} 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.",

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year = "2008",

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T1 - Structure of a 6-pyruvoyltetrahydropterin synthase homolog from Streptomyces coelicolor

AU - Spoonamore, James E.

AU - Roberts, Sue A.

AU - Heroux, Annie

AU - Bandarian, Vahe

PY - 2008

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AB - 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.

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KW - Streptomyces coelicolor

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Structure of a 6-pyruvoyltetrahydropterin synthase homolog from Streptomyces coelicolor

Abstract

Keywords

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