3WIA
Crystal structure of the N-terminal 1-37 residues deleted mutant of Geobacillus copper nitrite reductase
Summary for 3WIA
Entry DOI | 10.2210/pdb3wia/pdb |
Related | 3WI9 |
Descriptor | Nitrite reductase, COPPER (II) ION, FORMIC ACID, ... (4 entities in total) |
Functional Keywords | cupredoxin-fold, trimer, nitrite reduction, oxidoreductase |
Biological source | Geobacillus kaustophilus |
Total number of polymer chains | 9 |
Total formula weight | 287197.92 |
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 Cited by 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: 24440558DOI: 10.1016/j.bbabio.2014.01.004 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.77 Å) |
Structure validation
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