1BAW

PLASTOCYANIN FROM PHORMIDIUM LAMINOSUM

Summary for 1BAW

• Entry DOI: 10.2210/pdb1baw/pdb
• Descriptor: PLASTOCYANIN, COPPER (II) ION, ZINC ION, ... (4 entities in total)
• Functional Keywords: electron transfer, cyanobacteria, blue copper protein
• Biological source: Phormidium laminosum
• Total number of polymer chains: 3
• Total formula weight: 34682.26

Authors

Bond, C.S.,Guss, J.M.,Freeman, H.C.,Wagner, M.J.,Howe, C.J.,Bendall, D.S. (deposition date: 1998-04-19, release date: 1999-03-02, Last modification date: 2024-02-07)

Primary citation

Bond, C.S.,Bendall, D.S.,Freeman, H.C.,Guss, J.M.,Howe, C.J.,Wagner, M.J.,Wilce, M.C.
The structure of plastocyanin from the cyanobacterium Phormidium laminosum.
Acta Crystallogr.,Sect.D, 55:414-421, 1999

PubMed Abstract: The crystal structure of the 'blue' copper protein plastocyanin from the cyanobacterium Phormidium laminosum has been solved and refined using 2.8 A X--ray data. P. laminosum plastocyanin crystallizes in space group P43212 with unit-cell dimensions a = 86.57, c = 91.47 A and with three protein molecules per asymmetric unit. The final residual R is 19.9%. The structure was solved using molecular replacement with a search model based on the crystal structure of a close homologue, Anabaena variabilis plastocyanin (66% sequence identity). The molecule of P. laminosum plastocyanin has 105 amino-acid residues. The single Cu atom is coordinated by the same residues - two histidines, a cysteine and a methionine - as in other plastocyanins. In the crystal structure, the three molecules of the asymmetric unit are related by a non-crystallographic threefold axis. A Zn atom lies between each pair of neighbouring molecules in this ensemble, being coordinated by a surface histidine residue of one molecule and by two aspartates of the other.

PubMed: 10089349
DOI: 10.1107/S0907444998012074

Experimental method

X-RAY DIFFRACTION (2.8 Å)