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Crystallization and preliminary X-ray analysis of the O-methyltransferase NovP from the novobiocin-biosynthetic cluster of Streptomyces spheroides

Crystals of recombinant NovP (subunit MW = 29 967 Da; 262 amino acids), an S-adenosyl-l-methionine-dependent O-methyltransferase from Streptomyces spheroides, were grown by vapour diffusion. The protein crystallized in space group P2, with unit-cell parameters a = 51.81, b = 46.04, c = 61.22 Å, β =...

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Detalles Bibliográficos
Autores principales: Stevenson, Clare E. M., Freel Meyers, Caren L., Walsh, Christopher T., Lawson, David M.
Formato: Texto
Lenguaje:English
Publicado: International Union of Crystallography 2007
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2330194/
https://www.ncbi.nlm.nih.gov/pubmed/17329822
http://dx.doi.org/10.1107/S1744309107008287
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author Stevenson, Clare E. M.
Freel Meyers, Caren L.
Walsh, Christopher T.
Lawson, David M.
author_facet Stevenson, Clare E. M.
Freel Meyers, Caren L.
Walsh, Christopher T.
Lawson, David M.
author_sort Stevenson, Clare E. M.
collection PubMed
description Crystals of recombinant NovP (subunit MW = 29 967 Da; 262 amino acids), an S-adenosyl-l-methionine-dependent O-methyltransferase from Streptomyces spheroides, were grown by vapour diffusion. The protein crystallized in space group P2, with unit-cell parameters a = 51.81, b = 46.04, c = 61.22 Å, β = 104.97°. Native data to a maximum resolution of 1.4 Å were collected from a single crystal at the synchrotron. NovP is involved in the biosynthesis of the aminocoumarin antibiotic novobiocin that targets the essential bacterial enzyme DNA gyrase.
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spelling pubmed-23301942008-05-12 Crystallization and preliminary X-ray analysis of the O-methyltransferase NovP from the novobiocin-biosynthetic cluster of Streptomyces spheroides Stevenson, Clare E. M. Freel Meyers, Caren L. Walsh, Christopher T. Lawson, David M. Acta Crystallogr Sect F Struct Biol Cryst Commun Crystallization Communications Crystals of recombinant NovP (subunit MW = 29 967 Da; 262 amino acids), an S-adenosyl-l-methionine-dependent O-methyltransferase from Streptomyces spheroides, were grown by vapour diffusion. The protein crystallized in space group P2, with unit-cell parameters a = 51.81, b = 46.04, c = 61.22 Å, β = 104.97°. Native data to a maximum resolution of 1.4 Å were collected from a single crystal at the synchrotron. NovP is involved in the biosynthesis of the aminocoumarin antibiotic novobiocin that targets the essential bacterial enzyme DNA gyrase. International Union of Crystallography 2007-02-28 /pmc/articles/PMC2330194/ /pubmed/17329822 http://dx.doi.org/10.1107/S1744309107008287 Text en © International Union of Crystallography 2007 http://journals.iucr.org/services/termsofuse.html This is an open-access article distributed under the terms described at http://journals.iucr.org/services/termsofuse.html.
spellingShingle Crystallization Communications
Stevenson, Clare E. M.
Freel Meyers, Caren L.
Walsh, Christopher T.
Lawson, David M.
Crystallization and preliminary X-ray analysis of the O-methyltransferase NovP from the novobiocin-biosynthetic cluster of Streptomyces spheroides
title Crystallization and preliminary X-ray analysis of the O-methyltransferase NovP from the novobiocin-biosynthetic cluster of Streptomyces spheroides
title_full Crystallization and preliminary X-ray analysis of the O-methyltransferase NovP from the novobiocin-biosynthetic cluster of Streptomyces spheroides
title_fullStr Crystallization and preliminary X-ray analysis of the O-methyltransferase NovP from the novobiocin-biosynthetic cluster of Streptomyces spheroides
title_full_unstemmed Crystallization and preliminary X-ray analysis of the O-methyltransferase NovP from the novobiocin-biosynthetic cluster of Streptomyces spheroides
title_short Crystallization and preliminary X-ray analysis of the O-methyltransferase NovP from the novobiocin-biosynthetic cluster of Streptomyces spheroides
title_sort crystallization and preliminary x-ray analysis of the o-methyltransferase novp from the novobiocin-biosynthetic cluster of streptomyces spheroides
topic Crystallization Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2330194/
https://www.ncbi.nlm.nih.gov/pubmed/17329822
http://dx.doi.org/10.1107/S1744309107008287
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