1tu2
From Proteopedia
(New page: 200px<br /><applet load="1tu2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tu2" /> '''THE COMPLEX OF NOSTOC CYTOCHROME F AND PLAST...) |
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| - | [[Image:1tu2.gif|left|200px]]<br /><applet load="1tu2" size=" | + | [[Image:1tu2.gif|left|200px]]<br /><applet load="1tu2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1tu2" /> | caption="1tu2" /> | ||
'''THE COMPLEX OF NOSTOC CYTOCHROME F AND PLASTOCYANIN DETERMIN WITH PARAMAGNETIC NMR. BASED ON THE STRUCTURES OF CYTOCHROME F AND PLASTOCYANIN, 10 STRUCTURES'''<br /> | '''THE COMPLEX OF NOSTOC CYTOCHROME F AND PLASTOCYANIN DETERMIN WITH PARAMAGNETIC NMR. BASED ON THE STRUCTURES OF CYTOCHROME F AND PLASTOCYANIN, 10 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The complex between cytochrome f and plastocyanin from the cyanobacterium | + | 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== | ==About this Structure== | ||
| - | 1TU2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.] with CU and HEC as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1TU2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.] with <scene name='pdbligand=CU:'>CU</scene> and <scene name='pdbligand=HEC:'>HEC</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TU2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Diaz-Moreno, I.]] | [[Category: Diaz-Moreno, I.]] | ||
[[Category: Diaz-Quintana, A.]] | [[Category: Diaz-Quintana, A.]] | ||
| - | [[Category: Rosa, M | + | [[Category: Rosa, M A.De la.]] |
[[Category: Ubbink, M.]] | [[Category: Ubbink, M.]] | ||
[[Category: CU]] | [[Category: CU]] | ||
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[[Category: pseudocontact shift]] | [[Category: pseudocontact shift]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:17:18 2008'' |
Revision as of 13:17, 21 February 2008
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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 and 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
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