1JXF

SOLUTION STRUCTURE OF REDUCED CU(I) PLASTOCYANIN FROM SYNECHOCYSTIS PCC6803

Summary for 1JXF

• Entry DOI: 10.2210/pdb1jxf/pdb
• Related: 1I0W 1I0Y 1JXD
• Descriptor: PLASTOCYANIN, COPPER (II) ION (2 entities in total)
• Functional Keywords: copper protein beta barrel electron transfer, proton transport
• Biological source: Synechocystis sp. PCC 6803
• Total number of polymer chains: 1
• Total formula weight: 10312.98

Authors

Bertini, I.,Bryant, D.A.,Ciurli, S.,Dikiy, A.,Fernandez, C.O.,Luchinat, C.,Safarov, N.,Vila, A.J.,Zhao, J. (deposition date: 2001-09-07, release date: 2001-09-26, Last modification date: 2024-05-22)

Primary citation

Bertini, I.,Bryant, D.A.,Ciurli, S.,Dikiy, A.,Fernandez, C.O.,Luchinat, C.,Safarov, N.,Vila, A.J.,Zhao, J.
Backbone dynamics of plastocyanin in both oxidation states. Solution structure of the reduced form and comparison with the oxidized state.
J.Biol.Chem., 276:47217-47226, 2001

PubMed Abstract: A model-free analysis based on (15)N R(1), (15)N R(2), and (15)N-(1)H nuclear Overhauser effects was performed on reduced (diamagnetic) and oxidized (paramagnetic) forms of plastocyanin from Synechocystis sp. PCC6803. The protein backbone is rigid, displaying a small degree of mobility in the sub-nanosecond time scale. The loops surrounding the copper ion, involved in physiological electron transfer, feature a higher extent of flexibility in the longer time scale in both redox states, as measured from D(2)O exchange of amide protons and from NH-H(2)O saturation transfer experiments. In contrast to the situation for other electron transfer proteins, no significant difference in the dynamic properties is found between the two redox forms. A solution structure was also determined for the reduced plastocyanin and compared with the solution structure of the oxidized form in order to assess possible structural changes related to the copper ion redox state. Within the attained resolution, the structure of the reduced plastocyanin is indistinguishable from that of the oxidized form, even though small chemical shift differences are observed. The present characterization provides information on both the structural and dynamic behavior of blue copper proteins in solution that is useful to understand further the role(s) of protein dynamics in electron transfer processes.

PubMed: 11509552
DOI: 10.1074/jbc.M100304200

Experimental method

SOLUTION NMR