The crystal structure of pseudoazurin from Alcaligenes faecalis S-6 determined at 2.9 A resolution.
The three-dimensional structure of pseudoazurin, a single copper-containing protein from Alcaligenes faecalis strain S-6, has been determined at 2.9 A resolution by X-ray crystallography. The sequences of two other pseudoazurins from Pseudomonas AM1 and Achromobacter cycloclastes may also be accommodated in this structure. The structure, an eight-stranded beta-barrel, resembles closely those of plastocyanin and azurin. It possesses two extra alpha-helices at the C-terminus, whereas azurins have an alpha-helical flap in the middle of their sequences.
D000421:Alcaligenes / Q000032:analysis*; D000595:Amino Acid Sequence; D001400:Azurin / Q000031:analogs & derivatives; D001426:Bacterial Proteins; D003300:Copper / Q000032:analysis; D003460:Crystallization; D004579:Electron Transport; D010970:Plastocyanin; D011487:Protein Conformation; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; C047163:pseudoazurin; D001400:Azurin; D003300:Copper; D010970:Plastocyanin