3WIA: Crystal Structure Of The N-terminal 1-37 Residues Deleted Mutant Of Geobacillus Copper Nitrite Reductase

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 1.3A and 1.8A, respectively. Both structures show a striking resemblance with the overall structure of the well-known CuNiRs composed of two Greek key beta-barrel domains; however, a remarkable structural difference was found in the N-terminal region. The unique region has one beta-strand and one alpha-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.
PDB ID: 3WIADownload
MMDB ID: 121644
PDB Deposition Date: 2013/9/9
Updated in MMDB: 2014/07
Experimental Method:
x-ray diffraction
Resolution: 1.77  Å
Source Organism:
Similar Structures:
Biological Unit for 3WIA: trimeric; determined by author and by software (PISA)
Molecular Components in 3WIA
Label Count Molecule
Proteins (3 molecules)
Nitrite Reductase
Molecule annotation
Chemicals (12 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB