Cloning, expression, crystallization and preliminary X-ray studies of the ferredoxin-NAD(P)+ reductase from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1

Pasqual Liauw, Tomohiro Mashiba, Marta Kopczak, Katrin Wiegand, Norifumi Muraki, Hisako Kubota, Yusuke Kawano, Masahiko Ikeuchi, Toshiharu Hase, Matthias Rögner, Genji Kurisu

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)

Abstract

Ferredoxin-NADP+ reductase (FNR) is a flavoenzyme that catalyses the reduction of NADP+ in the final step of the photosynthetic electron-transport chain. FNR from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1 (TeFNR) contains an additional 9 kDa domain at its N-terminus relative to chloroplastic FNRs and is more thermostable than those from mesophilic cyanobacteria. With the aim of understanding the structural basis of the thermostability of TeFNR and assigning a structural role to the small additional domain, the gene encoding TeFNR with and without an additional domain was engineered for heterologous expression and the recombinant proteins were purified and crystallized. Crystals of TeFNR without the additional domain belonged to space group P21, with unit-cell parameters a = 55.05, b = 71.66, c = 89.73 Å, = 90, Β = 98.21, γ= 90°.

Original languageEnglish
Pages (from-to)1048-1051
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume68
Issue number9
DOIs
Publication statusPublished - 2012 Sep
Externally publishedYes

Keywords

  • electron-transfer complexes
  • ferredoxin
  • ferredoxin-NADP reductase

ASJC Scopus subject areas

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

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