2JXM
Ensemble of twenty structures of the Prochlorothrix hollandica plastocyanin- cytochrome f complex
Summary for 2JXM
| Entry DOI | 10.2210/pdb2jxm/pdb |
| Related | 1B3I 1CI3 |
| Descriptor | Plastocyanin, Cytochrome f, COPPER (II) ION, ... (4 entities in total) |
| Functional Keywords | copper, electron transport, metal-binding, transport |
| Biological source | Prochlorothrix hollandica More |
| Total number of polymer chains | 2 |
| Total formula weight | 37442.19 |
| Authors | Hulsker, R.,Baranova, M.,Bullerjahn, G.,Ubbink, M. (deposition date: 2007-11-22, release date: 2008-02-12, Last modification date: 2024-05-29) |
| Primary citation | Hulsker, R.,Baranova, M.V.,Bullerjahn, G.S.,Ubbink, M. Dynamics in the transient complex of plastocyanin-cytochrome f from Prochlorothrix hollandica. J.Am.Chem.Soc., 130:1985-1991, 2008 Cited by PubMed Abstract: The nature of transient protein complexes can range from a highly dynamic ensemble of orientations to a single well-defined state. This represents variation in the equilibrium between the encounter and final, functional state. The transient complex between plastocyanin (Pc) and cytochrome f (cytf) of the cyanobacterium Prochlorothrix hollandica was characterized by NMR spectroscopy. Intermolecular pseudocontact shifts and chemical shift perturbations were used as restraints in docking calculations to determine the structure of the wild-type Pc-cytf complex. The orientation of Pc is similar to orientations found in Pc-cytf complexes from other sources. Electrostatics seems to play a modest role in complex formation. A large variability in the ensemble of lowest energy structures indicates a dynamic nature of the complex. Two unusual hydrophobic patch residues in Pc have been mutated to the residues found in other plastocyanins (Y12G/P14L). The binding constants are similar for the complexes of cytf with wild-type Pc and mutant Pc, but the chemical shift perturbations are smaller for the complex with mutant Pc. Docking calculations for the Y12G/P14L Pc-cytf complex did not produce a converged ensemble of structures. Simulations of the dynamics were performed using the observed averaged NMR parameters as input. The results indicate a surprisingly large amplitude of mobility of Y12G/P14L Pc within the complex. It is concluded that the double mutation shifts the complex further from the well-defined toward the encounter state. PubMed: 18201089DOI: 10.1021/ja077453p PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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