1tu2
From Proteopedia
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THE COMPLEX OF NOSTOC CYTOCHROME F AND PLASTOCYANIN DETERMIN WITH PARAMAGNETIC NMR. BASED ON THE STRUCTURES OF CYTOCHROME F AND PLASTOCYANIN, 10 STRUCTURES
Overview
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 angstroms. 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.
About this Structure
1TU2 is a Protein complex structure of sequences from Anabaena sp. with CU and HEC as ligands. Full crystallographic information is available from OCA.
Reference
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., Diaz-Moreno I, Diaz-Quintana A, De la Rosa MA, Ubbink M, J Biol Chem. 2005 May 13;280(19):18908-15. Epub 2005 Feb 10. PMID:15705583
Page seeded by OCA on Wed Nov 21 03:35:29 2007
