5X31
Pseudoazurin from Alcaligenes faecalis (space group P65)
Summary for 5X31
| Entry DOI | 10.2210/pdb5x31/pdb |
| Descriptor | Pseudoazurin, COPPER (II) ION (3 entities in total) |
| Functional Keywords | cupredoxin, pseudoazurin, copper, electron transfer, electron transport |
| Biological source | Alcaligenes faecalis |
| Total number of polymer chains | 2 |
| Total formula weight | 27472.82 |
| Authors | Fukuda, Y.,Mizohata, E.,Inoue, T. (deposition date: 2017-02-03, release date: 2017-04-12, Last modification date: 2023-11-22) |
| Primary citation | Fukuda, Y.,Mizohata, E.,Inoue, T. New molecular packing in a crystal of pseudoazurin from Alcaligenes faecalis: a double-helical arrangement of blue copper Acta Crystallogr F Struct Biol Commun, 73:159-166, 2017 Cited by PubMed Abstract: Pseudoazurin from the denitrifying bacterium Alcaligenes faecalis (AfPAz) is a blue copper protein and functions as an electron donor to copper-containing nitrite reductase (CuNIR). Conventionally, AfPAz has been crystallized using highly concentrated ammonium sulfate as a precipitant. Here, a needle-like crystal of AfPAz grown in a solution containing a macromolecular precipitant, polyethylene glycol 8000 (PEG 8000), is reported. The crystal belonged to space group P6, with unit-cell parameters a = b = 68.7, c = 94.2 Å. The structure has been determined and refined at 2.6 Å resolution. The asymmetric unit contained two AfPAz molecules contacting each other on negatively charged surfaces. The molecular packing of the crystal showed a right-handed double-helical arrangement of AfPAz molecules and hence of blue copper sites. This structure provides insight into the excluded-volume effect of PEG and the manner of assembly of AfPAz. PubMed: 28291752DOI: 10.1107/S2053230X17002631 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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