1TU2
THE COMPLEX OF NOSTOC CYTOCHROME F AND PLASTOCYANIN DETERMIN WITH PARAMAGNETIC NMR. BASED ON THE STRUCTURES OF CYTOCHROME F AND PLASTOCYANIN, 10 STRUCTURES
Summary for 1TU2
| Entry DOI | 10.2210/pdb1tu2/pdb |
| Descriptor | Plastocyanin, Apocytochrome f, COPPER (II) ION, ... (4 entities in total) |
| Functional Keywords | electron transport, paramagnetic, chemical shift, complex formation, dynamic complex, photosynthesis, pseudocontact shift, electron transport proteins complex |
| Biological source | Nostoc sp. More |
| Cellular location | Cellular thylakoid membrane; Single-pass membrane protein (By similarity): Q93SW9 |
| Total number of polymer chains | 2 |
| Total formula weight | 39044.00 |
| Authors | Diaz-Moreno, I.,Diaz-Quintana, A.,De la Rosa, M.A.,Ubbink, M. (deposition date: 2004-06-24, release date: 2005-03-01, Last modification date: 2024-05-01) |
| Primary citation | Diaz-Moreno, I.,Diaz-Quintana, A.,De la Rosa, M.A.,Ubbink, M. 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. J.Biol.Chem., 280:18908-18915, 2005 Cited by PubMed Abstract: 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. PubMed: 15705583DOI: 10.1074/jbc.M413298200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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