2jxm

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(New page: 200px<br /><applet load="2jxm" size="350" color="white" frame="true" align="right" spinBox="true" caption="2jxm" /> '''Ensemble of twenty structures of the Prochlo...)
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==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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[[Category: transport]]
[[Category: transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 13 08:19:31 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:06:25 2008''

Revision as of 16:06, 21 February 2008


2jxm

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Ensemble of twenty structures of the Prochlorothrix hollandica plastocyanin- cytochrome f complex

Overview

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.

About this Structure

2JXM is a Protein complex structure of sequences from Prochlorothrix hollandica with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Dynamics in the transient complex of plastocyanin-cytochrome f from Prochlorothrix hollandica., Hulsker R, Baranova MV, Bullerjahn GS, Ubbink M, J Am Chem Soc. 2008 Feb 13;130(6):1985-91. Epub 2008 Jan 18. PMID:18201089

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