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 3D structure of the apo-pseudoazurin (copper free pseudoazurin) from Alcaligenes faecalis strain S-6 is determined and refined at pH 6.7 using X-ray diffraction data to 1.85 A resolution. The final crystallographic R-factor is 0.164. Comparing the structures of apo-pseudoazurin and the native (Cu2+) protein, we observed limited differences ranging between 0.1-0.4 A at the vicinity of the copper site, at the loops connecting the secondary structural elements, at certain beta-strands and at the amino and carboxy termini of the protein.
The crystal structure of apo-pseudoazurin from Alcaligenes faecalis S-6.,Petratos K, Papadovasilaki M, Dauter Z FEBS Lett. 1995 Jul 24;368(3):432-4. PMID:7635192[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Petratos K, Papadovasilaki M, Dauter Z. The crystal structure of apo-pseudoazurin from Alcaligenes faecalis S-6. FEBS Lett. 1995 Jul 24;368(3):432-4. PMID:7635192
