Structure of a 6-pyruvoyltetrahydropterin synthase homolog from Streptomyces coelicolor

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

Research output: Contribution to journalArticle

2 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)875-879
Number of pages5
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume64
Issue number10
DOIs
StatePublished - 2008

Fingerprint

Streptomyces coelicolor
Catalytic Domain
activity (biology)
Pterins
metal ions
zinc
Bioactivity
proteins
crystal structure
Metal ions
Zinc
Crystal structure
Metals
X-Rays
Ions
X rays
x rays
Substrates
6-pyruvoyltetrahydropterin synthase
Proteins

Keywords

  • 6-pyruvoyltetrahydropterin synthase homolog
  • SCO 6650
  • Streptomyces coelicolor

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Structural Biology
  • Genetics
  • Condensed Matter Physics

Cite this

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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.",
keywords = "6-pyruvoyltetrahydropterin synthase homolog, SCO 6650, Streptomyces coelicolor",
author = "Spoonamore, {James E.} and Roberts, {Sue A} and Annie Heroux and Vahe Bandarian",
year = "2008",
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journal = "Acta Crystallographica Section F:Structural Biology Communications",
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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

Y1 - 2008

N2 - 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.

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 - SCO 6650

KW - Streptomyces coelicolor

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