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

Clare E M Stevenson, Caren L Meyers, Christopher T. Walsh, David M. Lawson

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish (US)
Pages (from-to)236-238
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume63
Issue number3
DOIs
StatePublished - Feb 13 2007

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Aminocoumarins
DNA Gyrase
Novobiocin
methionine
Bacterial DNA
Synchrotrons
biosynthesis
antibiotics
Biosynthesis
X ray analysis
Methyltransferases
Streptomyces
Crystallization
Methionine
amino acids
enzymes
synchrotrons
deoxyribonucleic acid
Vapors
X-Rays

Keywords

  • Antibiotic biosynthesis
  • Novobiocin
  • NovP
  • O-methyltransferase
  • Streptomyces

ASJC Scopus subject areas

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

Cite this

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title = "Crystallization and preliminary X-ray analysis of the O-methyltransferase NovP from the novobiocin-biosynthetic cluster of Streptomyces spheroides",
abstract = "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 {\AA}, β = 104.97°. Native data to a maximum resolution of 1.4 {\AA} 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.",
keywords = "Antibiotic biosynthesis, Novobiocin, NovP, O-methyltransferase, Streptomyces",
author = "Stevenson, {Clare E M} and Meyers, {Caren L} and Walsh, {Christopher T.} and Lawson, {David M.}",
year = "2007",
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doi = "10.1107/S1744309107008287",
language = "English (US)",
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pages = "236--238",
journal = "Acta Crystallographica Section F:Structural Biology Communications",
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publisher = "John Wiley and Sons Ltd",
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T1 - Crystallization and preliminary X-ray analysis of the O-methyltransferase NovP from the novobiocin-biosynthetic cluster of Streptomyces spheroides

AU - Stevenson, Clare E M

AU - Meyers, Caren L

AU - Walsh, Christopher T.

AU - Lawson, David M.

PY - 2007/2/13

Y1 - 2007/2/13

N2 - 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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KW - Antibiotic biosynthesis

KW - Novobiocin

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KW - Streptomyces

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