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Structure of a 6‐pyruvoyltetrahydropterin synthase homolog from Streptomyces coelicolor

Structure of a 6‐pyruvoyltetrahydropterin synthase homolog from Streptomyces coelicolor 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Structure of a 6‐pyruvoyltetrahydropterin synthase homolog from Streptomyces coelicolor

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References (17)

Publisher
Wiley
Copyright
International Union of Crystallography, 2008
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309108027048
pmid
18931427
Publisher site
See Article on Publisher Site

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.

Journal

Acta Crystallographica Section FWiley

Published: Oct 1, 2008

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