Pseudoazurin-nitrite reductase interactions.
The nitrite reductase-binding site on pseudoazurin has been determined by using NMR chemical-shift perturbations. It comprises residues in the hydrophobic patch surrounding the exposed copper ligand His81 as well as several positively charged residues. The binding site is similar for both redox states of pseudoazurin, despite differences in the binding mode. The results suggest that pseudoazurin binds in a well-defined orientation. Docking simulations provide a putative structure of the complex with a binding site on nitrite reductase that has several hydrophobic and polar residues as well as a ridge of negatively charged side chains and a copper-to-copper distance of 14 A.
Impagliazzo
Antonietta
A
Leiden Institute of Chemistry, Leiden University, P.O. Box 9502, 2300RA Leiden, The Netherlands.
Krippahl
Ludwig
L
Ubbink
Marcellus
M
D001400:Azurin / Q000737:chemistry* / Q000378:metabolism*; D003300:Copper / Q000737:chemistry; D008958:Models, Molecular; D009572:Nitrite Reductases / Q000737:chemistry* / Q000378:metabolism*; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D020836:Protein Structure, Quaternary
C047163:pseudoazurin; D001400:Azurin; D003300:Copper; D009572:Nitrite Reductases