Crystallization and preliminary crystallographic analysis of the complex between triiodothyronine and the bb′ fragment of rat protein disulfide isomerase

Shoko Hashimoto, Len Ito, Masaki Okumura, Tomohisa Shibano, Marina Nawata, Takashi Kumasaka, Hiroshi Yamaguchi, Susumu Imaoka

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Protein disulfide isomerase (PDI) is a multifunctional protein that catalyzes the formation of a disulfide bond in nascent and misfolded proteins and is also known to bind to the thyroid hormone triiodothyronine (T3). When T3 is bound to PDI its catalytic activity is inhibited, but the biological function of this binding is not well understood. In previous studies, it was found that T3 binds to the bb′ fragment of PDI. Therefore, to clarify the structure of the complex consisting of PDI bound to T3, a crystallographic analysis of the three-dimensional structure of the T3-rat PDI bb′ complex was performed. Native bb′ crystals and T3-bb′ complex crystals were both obtained using the hanging-drop vapour-diffusion technique with 1.6 M trisodium citrate pH 6.2 as a precipitant. The space group of the native bb′ crystals was found to be C222, with unit-cell parameters a = 94.8, b = 114.9, c = 182.9 Å, while the space group of the T3-bb′ complex crystals was P2 12121, with unit-cell parameters a = 99.9, b = 184.5, c = 232.2 Å. Diffraction data for the native and complex crystals were collected to resolutions of 3.06 and 3.00 Å, respectively.

Original languageEnglish
Pages (from-to)476-478
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume68
Issue number4
DOIs
Publication statusPublished - 2012 Apr 1

Keywords

  • Bb′ fragment
  • Bisphenol A
  • Protein disulfide isomerase
  • Triiodothyronine

ASJC Scopus subject areas

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

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