Crystallization and preliminary X-ray crystallographic studies of a new class of enoyl-(acyl-carrier protein) reductase, FabV, from Vibrio fischeri

Ae Kyung Park, Jeong Hye Lee, Young Min Chi, Jin Ho Moon

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Enoyl-(acyl-carrier protein) reductase (ENR) catalyzes the last step of the fatty-acid elongation cycle of the bacterial fatty-acid biosynthesis (FAS II) pathway. Recently, a new class of ENR has been identified from Vibrio cholerae and was named FabV. In order to understand the molecular mechanism of the new class of ENR at the structural level, FabV from V. fischeri was overexpressed, purified and crystallized. Diffraction data were collected to 2.7 Å resolution from a native crystal. The crystal belonged to the orthorhombic space group P21212, with unit-cell parameters a = 123.53, b = 164.14, c = 97.07 Å. The presence of four molecules of FabV in the asymmetric unit gave a V M value of 2.81 Å 3 Da -1, with a corresponding solvent content of 54.5%.

Original languageEnglish
Pages (from-to)78-80
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume68
Issue number1
DOIs
Publication statusPublished - 2012 Jan 1

Fingerprint

Aliivibrio fischeri
Acyl Carrier Protein
Crystallization
Oxidoreductases
X-Rays
fatty acids
crystallization
proteins
X rays
Fatty Acids
cholera
Crystals
biosynthesis
x rays
Vibrio cholerae
Biosynthesis
elongation
crystals
Elongation
Diffraction

Keywords

  • enoyl-(acyl-carrier protein) reductase
  • FabV
  • FAS II pathway
  • Vibrio fischeri

ASJC Scopus subject areas

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

Cite this

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abstract = "Enoyl-(acyl-carrier protein) reductase (ENR) catalyzes the last step of the fatty-acid elongation cycle of the bacterial fatty-acid biosynthesis (FAS II) pathway. Recently, a new class of ENR has been identified from Vibrio cholerae and was named FabV. In order to understand the molecular mechanism of the new class of ENR at the structural level, FabV from V. fischeri was overexpressed, purified and crystallized. Diffraction data were collected to 2.7 {\AA} resolution from a native crystal. The crystal belonged to the orthorhombic space group P21212, with unit-cell parameters a = 123.53, b = 164.14, c = 97.07 {\AA}. The presence of four molecules of FabV in the asymmetric unit gave a V M value of 2.81 {\AA} 3 Da -1, with a corresponding solvent content of 54.5{\%}.",
keywords = "enoyl-(acyl-carrier protein) reductase, FabV, FAS II pathway, Vibrio fischeri",
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T1 - Crystallization and preliminary X-ray crystallographic studies of a new class of enoyl-(acyl-carrier protein) reductase, FabV, from Vibrio fischeri

AU - Park, Ae Kyung

AU - Lee, Jeong Hye

AU - Chi, Young Min

AU - Moon, Jin Ho

PY - 2012/1/1

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N2 - Enoyl-(acyl-carrier protein) reductase (ENR) catalyzes the last step of the fatty-acid elongation cycle of the bacterial fatty-acid biosynthesis (FAS II) pathway. Recently, a new class of ENR has been identified from Vibrio cholerae and was named FabV. In order to understand the molecular mechanism of the new class of ENR at the structural level, FabV from V. fischeri was overexpressed, purified and crystallized. Diffraction data were collected to 2.7 Å resolution from a native crystal. The crystal belonged to the orthorhombic space group P21212, with unit-cell parameters a = 123.53, b = 164.14, c = 97.07 Å. The presence of four molecules of FabV in the asymmetric unit gave a V M value of 2.81 Å 3 Da -1, with a corresponding solvent content of 54.5%.

AB - Enoyl-(acyl-carrier protein) reductase (ENR) catalyzes the last step of the fatty-acid elongation cycle of the bacterial fatty-acid biosynthesis (FAS II) pathway. Recently, a new class of ENR has been identified from Vibrio cholerae and was named FabV. In order to understand the molecular mechanism of the new class of ENR at the structural level, FabV from V. fischeri was overexpressed, purified and crystallized. Diffraction data were collected to 2.7 Å resolution from a native crystal. The crystal belonged to the orthorhombic space group P21212, with unit-cell parameters a = 123.53, b = 164.14, c = 97.07 Å. The presence of four molecules of FabV in the asymmetric unit gave a V M value of 2.81 Å 3 Da -1, with a corresponding solvent content of 54.5%.

KW - enoyl-(acyl-carrier protein) reductase

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