3WI9

Crystal structure of copper nitrite reductase from Geobacillus kaustophilus

Summary for 3WI9

• Entry DOI: 10.2210/pdb3wi9/pdb
• Related: 3WIA
• Descriptor: Nitrite reductase, COPPER (II) ION, ZINC ION, ... (8 entities in total)
• Functional Keywords: cupredoxin-fold, trimer, nitrite reduction, oxidoreductase
• Biological source: Geobacillus kaustophilus
• Total number of polymer chains: 1
• Total formula weight: 36156.62

Authors

Fukuda, Y.,Nojiri, M. (deposition date: 2013-09-09, release date: 2014-07-23, Last modification date: 2023-11-08)

Primary citation

Fukuda, Y.,Koteishi, H.,Yoneda, R.,Tamada, T.,Takami, H.,Inoue, T.,Nojiri, M.
Structural and functional characterization of the Geobacillus copper nitrite reductase: involvement of the unique N-terminal region in the interprotein electron transfer with its redox partner
Biochim.Biophys.Acta, 1837:396-405, 2014

PubMed Abstract: The crystal structures of copper-containing nitrite reductase (CuNiR) from the thermophilic Gram-positive bacterium Geobacillus kaustophilus HTA426 and the amino (N)-terminal 68 residue-deleted mutant were determined at resolutions of 1.3Å and 1.8Å, respectively. Both structures show a striking resemblance with the overall structure of the well-known CuNiRs composed of two Greek key β-barrel domains; however, a remarkable structural difference was found in the N-terminal region. The unique region has one β-strand and one α-helix extended to the northern surface of the type-1 copper site. The superposition of the Geobacillus CuNiR model on the electron-transfer complex structure of CuNiR with the redox partner cytochrome c551 in other denitrifier system led us to infer that this region contributes to the transient binding with the partner protein during the interprotein electron transfer reaction in the Geobacillus system. Furthermore, electron-transfer kinetics experiments using N-terminal residue-deleted mutant and the redox partner, Geobacillus cytochrome c551, were carried out. These structural and kinetics studies demonstrate that the region is directly involved in the specific partner recognition.

PubMed: 24440558
DOI: 10.1016/j.bbabio.2014.01.004

Experimental method

X-RAY DIFFRACTION (1.3 Å)