2GIM

1.6 Angstrom structure of plastocyanin from Anabaena variabilis

Summary for 2GIM

• Entry DOI: 10.2210/pdb2gim/pdb
• Descriptor: Plastocyanin, COPPER (II) ION (3 entities in total)
• Functional Keywords: beta sheet, cu, helix, electron transport
• Biological source: Anabaena variabilis
• Cellular location: Cellular thylakoid membrane ; Peripheral membrane protein ; Lumenal side : P0C178
• Total number of polymer chains: 2
• Total formula weight: 22622.77

Authors

Schmidt, L.,Harris, P.,Christensen, H.E.M. (deposition date: 2006-03-29, release date: 2006-04-11, Last modification date: 2023-08-30)

Primary citation

Schmidt, L.,Christensen, H.E.,Harris, P.
Structure of plastocyanin from the cyanobacterium Anabaena variabilis.
ACTA CRYSTALLOGR.,SECT.D, 62:1022-1029, 2006

PubMed Abstract: Plastocyanin from the cyanobacterium Anabaena variabilis was heterologously produced in Escherichia coli and purified. Plate-like crystals were obtained by crystallization in 1.15 M trisodium citrate and 7.67 mM sodium borate buffer pH 8.5. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 67.85, b = 45.81, c = 63.41 Angstrom. The structure of the oxidized protein was solved to a resolution of 1.6 Angstrom using plastocyanin from Phormidium laminosum as a 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 there were two distinct conformations of His61.

PubMed: 16929103
DOI: 10.1107/S0907444906023638

Experimental method

X-RAY DIFFRACTION (1.6 Å)