Literature DB >> 18931427

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

James E Spoonamore1, Sue A Roberts, Annie Heroux, Vahe Bandarian.   

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.

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Year:  2008        PMID： 18931427      PMCID： PMC2564891          DOI： 10.1107/S1744309108027048

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN： 1744-3091


  22 in total

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Journal:  Nature       Date:  2002-05-09       Impact factor: 49.962

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10.  6-Pyruvoyl tetrahydropterin synthase, an enzyme with a novel type of active site involving both zinc binding and an intersubunit catalytic triad motif; site-directed mutagenesis of the proposed active center, characterization of the metal binding site and modelling of substrate binding.

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Journal:  J Mol Biol       Date:  1995-10-20       Impact factor: 5.469
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