Structural highlights
Function
[AZUP_ALCFA] This soluble electron transfer copper protein is required for the inactivation of copper-containing nitrite reductase in the presence of oxygen. Serves as a direct electron donor to the nitrite reductase.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structures of the reduced (Cu1+) blue-copper protein pseudoazurin from Alcaligenes faecalis strain S-6 are refined at pH 7.8 and 4.4 using X-ray diffraction data to 1.8 A resolution. The final R-factors for the high and low pH structures are 0.178 and 0.177, respectively. Comparing the reduced pseudoazurin at pH 7.8 with the oxidised (Cu2+) molecule, small changes are observed in the vicinity of the copper site and on the protein surface. At pH 4.4 the copper substituent imidazole of His81 rotates away from the metal with a concurrent movement of the latter towards the plane of the remaining three ligands (S gamma-Cys78, N delta 1-His40 and S delta-Met86) thus the geometry of the copper site becomes planar trigonal.
The crystal structures of reduced pseudoazurin from Alcaligenes faecalis S-6 at two pH values.,Vakoufari E, Wilson KS, Petratos K FEBS Lett. 1994 Jun 27;347(2-3):203-6. PMID:8034003[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Vakoufari E, Wilson KS, Petratos K. The crystal structures of reduced pseudoazurin from Alcaligenes faecalis S-6 at two pH values. FEBS Lett. 1994 Jun 27;347(2-3):203-6. PMID:8034003
