Crystallization and preliminary X-ray crystallographic analysis of the methionine sulfoxide reductase A domain of MsrAB from Haemophilus influenzae

Ah Reum Han, Hyun Sook Kim, Gye Yoon Cho, Ho Sam Ki, Hwa Young Kim, Kwang Yeon Hwang

Research output: Contribution to journalArticle

Abstract

Methionine sulfoxide reductase (Msr) is a repair enzyme that reduces oxidized methionine to methionine. The Msr enzyme is divided into MsrA and MsrB, which reduce the S and R configurations of the substrate, respectively. In some pathogenic bacteria MsrA and MsrB exist in a fusion-protein form, MsrAB. In this study, the recombinant MsrA part of MsrAB from Haemophilus influenzae (HIMsrA) was overexpressed, purified and crystallized using the hanging-drop vapour-diffusion method. A diffraction data set was collected to 1.6 Å resolution. The crystal of HIMsrA was found to belong to space group P41212, with unit-cell parameters a = b = 57.29, c = 186.28 Å, a calculated Matthews coefficient of 1.82 Å 3 Da -1 and two molecules per asymmetric unit. A preliminary solution was determined by molecular replacement. Refinement of the structure is currently in progress.

Original languageEnglish
Pages (from-to)557-559
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume68
Issue number5
DOIs
Publication statusPublished - 2012 May 1

Keywords

  • Haemophilus influenzae
  • MsrAB
  • Reactive oxygen species
  • Reductases

ASJC Scopus subject areas

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

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