Crystallization and preliminary X-ray studies of ferredoxin-NAD(P)+ reductase from Chlorobium tepidum

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Mar 1;64(Pt 3):186-9. doi: 10.1107/S1744309108003667. Epub 2008 Feb 23.

Abstract

Ferredoxin-NAD(P)(+) reductase (FNR) is a key enzyme that catalyzes the photoreduction of NAD(P)(+) to generate NAD(P)H during the final step of the photosynthetic electron-transport chain. FNR from the green sulfur bacterium Chlorobium tepidum is a homodimeric enzyme with a molecular weight of 90 kDa; it shares a high level of amino-acid sequence identity to thioredoxin reductase rather than to conventional plant-type FNRs. In order to understand the structural basis of the ferredoxin-dependency of this unique photosynthetic FNR, C. tepidum FNR has been heterologously expressed, purified and crystallized in two forms. Form I crystals belong to space group C222(1) and contain one dimer in the asymmetric unit, while form II crystals belong to space group P4(1)22 or P4(3)22. Diffraction data were collected from a form I crystal to 2.4 A resolution on the synchrotron-radiation beamline NW12 at the Photon Factory.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chlorobium / enzymology*
  • Chlorobium / genetics
  • Crystallization
  • Ferredoxin-NADP Reductase / chemistry*
  • Ferredoxin-NADP Reductase / genetics
  • Ferredoxin-NADP Reductase / metabolism*
  • X-Ray Diffraction

Substances

  • Ferredoxin-NADP Reductase