5I5I: Shewanella Denitrificans Nitrous Oxide Reductase, App Form

The copper enzyme nitrous oxide reductase catalyzes the two-electron reduction of nitrous oxide N(2)O to dinitrogen N(2). Its maturation largely occurs in the periplasm and includes the insertion of at least one Ca(2)(+) ion per monomer. Here we have investigated the role of this structural cation in recombinantly produced apo-N(2)OR from Shewanella denitrificans and have determined the three-dimensional structure of the protein by X-ray crystallography. In the absence of Ca(2)(+), substantial parts of the enzyme surrounding the binding sites for the copper ions show structural disorder. Reconstitution of the binuclear CuA site was possible in vitro but required the presence of Ca(2)(+) ions for a stable insertion of the center. In contrast, an excess of Ca(2)(+) prevented copper insertion, and the structural analysis of the Ca(2)(+)apo form revealed that the cation is sufficient to structure the disordered regions of the protein even in the absence of Cu ions, indicating that the geometry of the two noncanonical copper centers is largely predetermined by the protein structure.
PDB ID: 5I5IDownload
MMDB ID: 137097
PDB Deposition Date: 2016/2/15
Updated in MMDB: 2017/09
Experimental Method:
x-ray diffraction
Resolution: 2.14  Å
Source Organism:
Similar Structures:
Biological Unit for 5I5I: dimeric; determined by software (PISA)
Molecular Components in 5I5I
Label Count Molecule
Proteins (2 molecules)
Nitrous-oxide Reductase
Molecule annotation
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Citing MMDB