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J. Biol. Chem., Vol. 280, Issue 19, 18908-18915, May 13, 2005

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Structure of the Complex between Plastocyanin and Cytochrome f from the Cyanobacterium Nostoc sp. PCC 7119 as Determined by Paramagnetic NMR

THE BALANCE BETWEEN ELECTROSTATIC AND HYDROPHOBIC INTERACTIONS WITHIN THE TRANSIENT COMPLEX DETERMINES THE RELATIVE ORIENTATION OF THE TWO PROTEINS^*

Irene Díaz-Moreno, Antonio Díaz-Quintana, Miguel A. De la Rosa, and Marcellus Ubbink¶

From the Instituto de Bioquímica Vegetal y Fotosíntesis, Universidad de Sevilla y Consejo Superior de Investigaciones Científicas, Avda. Américo Vespucio 49, 41092 Sevilla, Spain, and Leiden Institute of Chemistry, Leiden University, Gorlaeus Laboratories, P. O. Box 9502, 2300 RA Leiden, The Netherlands

The complex between cytochrome f and plastocyanin from the cyanobacterium Nostoc has been characterized by NMR spectroscopy. The binding constant is 16 mM^–1, and the lifetime of the complex is much less than 10 ms. Intermolecular pseudo-contact shifts observed for the plastocyanin amide nuclei, caused by the heme iron, as well as the chemical-shift perturbation data were used as the sole experimental restraints to determine the orientation of plastocyanin relative to cytochrome f with a precision of 1.3 Å. The data show that the hydrophobic patch surrounding tyrosine 1 in cytochrome f docks the hydrophobic patch of plastocyanin. Charge complementarities are found between the rims of the respective recognition sites of cytochrome f and plastocyanin. Significant differences in the relative orientation of both proteins are found between this complex and those previously reported for plants and Phormidium, indicating that electrostatic and hydrophobic interactions are balanced differently in these complexes.

Received for publication, November 25, 2004 , and in revised form, February 3, 2005.

^* This work was supported by Program Human Potential and Mobility of Researchers of the European Commission Contract HPRN-CT-1999-00095 "Transient Network," Spanish Ministry of Education, Culture, and Sport Grant AP2000-2937, Spanish Ministry of Science and Technology Grant BMC2003-00458, the Andalusian Government Grant CVI-0198, and Netherlands Organization for Scientific Research Grant 700.52.425. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental material.

The atomic coordinates and structure factors (code 1TU2) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^¶ To whom correspondence should be addressed. Tel.: 31-71-527-4628; Fax: 31-71-527-4349; E-mail: m.ubbink{at}chem.leidenuniv.nl.

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