Journal article
Structure of plastocyanin from the cyanobacterium Anabaena variabilis
Plastocyanin from the cyanobacterium Anabaena variabilis was heterologously produced in E. coli and purified. Plate-like crystals were obtained by crystallisation in 1.15 M trisodium citrate and 7.67 mM sodium borate buffer pH 8.5. The crystals belong to the orthorhombic space group P212121 with cell dimensions a = 67.85 Å, b = 45.81 Å and c = 63.41 Å.
The structure of the oxidised protein was solved to a resolution of 1.6 Å using plastocyanin from Phormidium laminosum as search model. Two molecules were found in the asymmetric unit. The electrostatic surface of the basic protein showed a large population of positively charged residues in the northern site, whereas the eastern site lacked the two strongly negatively charged patches.
The copper ion was found to be relatively mobile and two distinct conformations of His61.
| Language: | English |
|---|---|
| Year: | 2006 |
| Pages: | 1022-1029 |
| ISSN: | 13990047 and 09074449 |
| Types: | Journal article |
| DOI: | 10.1107/S0907444906023638 |
| ORCIDs: | Christensen, Hans Erik Mølager and Harris, Pernille |
Amino Acid Sequence Anabaena Borates Citrates Crystallization Crystallography, X-Ray Electrons Escherichia coli Hydrogen-Ion Concentration Molecular Conformation Molecular Sequence Data Plastocyanin Protein Conformation Protein Structure, Secondary Sequence Homology, Amino Acid Static Electricity sodium borate trisodium citrate
