Crystallization and preliminary X-ray crystallographic analysis of MxaJ, a component of the methanol-oxidizing system operon from the marine bacterium Methylophaga aminisulfidivorans MPT

Jin Myung Choi, Jung Hun Kang, Dong Woo Lee, Si Wouk Kim, Sung Haeng Lee

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3 Citations (Scopus)

Abstract

The methanol-oxidizing system (mox) is essential for methylotrophic bacteria to extract energy during the oxidoreduction reaction and consists of a series of electron-transfer proteins encoded by the mox operon. One of the key enzymes is the 2β2 methanol dehydrogenase complex (type I MDH), which converts methanol to formaldehyde during the 2e- transfer through the prosthetic group pyrroloquinoline quinone. MxaJ, a product of mxaJ of the mox operon, is a component of the MDH complex and enhances the methanol-converting activity of the MDH complex. However, the exact functional mechanism of MxaJ in the complex is not clearly known. To investigate the functional role of MxaJ in MDH activity, an attempt was made to determine its crystal structure. Diffraction data were collected from a selenomethionine-substituted crystal to 1.92Å resolution at the peak wavelength. The crystal belonged to the orthorhombic space group P212121, with unit-cell parameters a = 37.127, b = 63.761, c = 99.246Å. The asymmetric unit contained one MxaJ molecule with a calculated Matthews coefficient of 2.11Å3Da-1 and a solvent content of 41.7%. Three-dimensional structure determination of the MxaJ protein is currently in progress by the single-wavelength anomalous dispersion technique and model building.

Original languageEnglish
Pages (from-to)902-905
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume69
Issue number8
DOIs
Publication statusPublished - 2013 Aug 1

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Operon
Crystallization
bacteria
Methanol
Bacteria
methyl alcohol
X-Rays
crystallization
X rays
x rays
PQQ Cofactor
Selenomethionine
Wavelength
Crystals
proteins
Prosthetics
dehydrogenases
Formaldehyde
quinones
formaldehyde

All Science Journal Classification (ASJC) codes

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

Cite this

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title = "Crystallization and preliminary X-ray crystallographic analysis of MxaJ, a component of the methanol-oxidizing system operon from the marine bacterium Methylophaga aminisulfidivorans MPT",
abstract = "The methanol-oxidizing system (mox) is essential for methylotrophic bacteria to extract energy during the oxidoreduction reaction and consists of a series of electron-transfer proteins encoded by the mox operon. One of the key enzymes is the 2β2 methanol dehydrogenase complex (type I MDH), which converts methanol to formaldehyde during the 2e- transfer through the prosthetic group pyrroloquinoline quinone. MxaJ, a product of mxaJ of the mox operon, is a component of the MDH complex and enhances the methanol-converting activity of the MDH complex. However, the exact functional mechanism of MxaJ in the complex is not clearly known. To investigate the functional role of MxaJ in MDH activity, an attempt was made to determine its crystal structure. Diffraction data were collected from a selenomethionine-substituted crystal to 1.92{\AA} resolution at the peak wavelength. The crystal belonged to the orthorhombic space group P212121, with unit-cell parameters a = 37.127, b = 63.761, c = 99.246{\AA}. The asymmetric unit contained one MxaJ molecule with a calculated Matthews coefficient of 2.11{\AA}3Da-1 and a solvent content of 41.7{\%}. Three-dimensional structure determination of the MxaJ protein is currently in progress by the single-wavelength anomalous dispersion technique and model building.",
author = "Choi, {Jin Myung} and Kang, {Jung Hun} and Lee, {Dong Woo} and Kim, {Si Wouk} and Lee, {Sung Haeng}",
year = "2013",
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T1 - Crystallization and preliminary X-ray crystallographic analysis of MxaJ, a component of the methanol-oxidizing system operon from the marine bacterium Methylophaga aminisulfidivorans MPT

AU - Choi, Jin Myung

AU - Kang, Jung Hun

AU - Lee, Dong Woo

AU - Kim, Si Wouk

AU - Lee, Sung Haeng

PY - 2013/8/1

Y1 - 2013/8/1

N2 - The methanol-oxidizing system (mox) is essential for methylotrophic bacteria to extract energy during the oxidoreduction reaction and consists of a series of electron-transfer proteins encoded by the mox operon. One of the key enzymes is the 2β2 methanol dehydrogenase complex (type I MDH), which converts methanol to formaldehyde during the 2e- transfer through the prosthetic group pyrroloquinoline quinone. MxaJ, a product of mxaJ of the mox operon, is a component of the MDH complex and enhances the methanol-converting activity of the MDH complex. However, the exact functional mechanism of MxaJ in the complex is not clearly known. To investigate the functional role of MxaJ in MDH activity, an attempt was made to determine its crystal structure. Diffraction data were collected from a selenomethionine-substituted crystal to 1.92Å resolution at the peak wavelength. The crystal belonged to the orthorhombic space group P212121, with unit-cell parameters a = 37.127, b = 63.761, c = 99.246Å. The asymmetric unit contained one MxaJ molecule with a calculated Matthews coefficient of 2.11Å3Da-1 and a solvent content of 41.7%. Three-dimensional structure determination of the MxaJ protein is currently in progress by the single-wavelength anomalous dispersion technique and model building.

AB - The methanol-oxidizing system (mox) is essential for methylotrophic bacteria to extract energy during the oxidoreduction reaction and consists of a series of electron-transfer proteins encoded by the mox operon. One of the key enzymes is the 2β2 methanol dehydrogenase complex (type I MDH), which converts methanol to formaldehyde during the 2e- transfer through the prosthetic group pyrroloquinoline quinone. MxaJ, a product of mxaJ of the mox operon, is a component of the MDH complex and enhances the methanol-converting activity of the MDH complex. However, the exact functional mechanism of MxaJ in the complex is not clearly known. To investigate the functional role of MxaJ in MDH activity, an attempt was made to determine its crystal structure. Diffraction data were collected from a selenomethionine-substituted crystal to 1.92Å resolution at the peak wavelength. The crystal belonged to the orthorhombic space group P212121, with unit-cell parameters a = 37.127, b = 63.761, c = 99.246Å. The asymmetric unit contained one MxaJ molecule with a calculated Matthews coefficient of 2.11Å3Da-1 and a solvent content of 41.7%. Three-dimensional structure determination of the MxaJ protein is currently in progress by the single-wavelength anomalous dispersion technique and model building.

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