1lfm
From Proteopedia
(New page: 200px<br /><applet load="1lfm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lfm, resolution 1.50Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1lfm.gif|left|200px]]<br /><applet load="1lfm" size=" | + | [[Image:1lfm.gif|left|200px]]<br /><applet load="1lfm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lfm, resolution 1.50Å" /> | caption="1lfm, resolution 1.50Å" /> | ||
'''CRYSTAL STRUCTURE OF COBALT(III)-SUBSTITUTED CYTOCHROME C (TUNA)'''<br /> | '''CRYSTAL STRUCTURE OF COBALT(III)-SUBSTITUTED CYTOCHROME C (TUNA)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Replacement of iron with cobalt(III) selectively introduces a deep trap in | + | Replacement of iron with cobalt(III) selectively introduces a deep trap in the folding-energy landscape of the heme protein cytochrome c. Remarkably, neither the protein structure nor the folding thermodynamics is perturbed by this metal-ion substitution, as shown by data from spectroscopic and x-ray diffraction experiments. Through kinetics measurements, we have found parallel folding pathways involving several different misligated Co(III) species, and, as these folding intermediates persist for several hours under certain conditions, we have been able to elucidate fully their spectroscopic properties. The results, along with an analysis of the fluorescence energy-transfer kinetics during refolding, show that rapidly equilibrating populations of compact and extended polypeptide conformations are present until all molecules have reached the native structure. These measurements provide direct evidence that collapsed denatured structures are not substantially more stable than extended conformations of cytochrome c. |
==About this Structure== | ==About this Structure== | ||
| - | 1LFM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thunnus_thynnus Thunnus thynnus] with COH as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1LFM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thunnus_thynnus Thunnus thynnus] with <scene name='pdbligand=COH:'>COH</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LFM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thunnus thynnus]] | [[Category: Thunnus thynnus]] | ||
| - | [[Category: Crane, B | + | [[Category: Crane, B R.]] |
| - | [[Category: Findley, W | + | [[Category: Findley, W M.]] |
| - | [[Category: Gray, H | + | [[Category: Gray, H B.]] |
| - | [[Category: Lyubovitsky, J | + | [[Category: Lyubovitsky, J G.]] |
| - | [[Category: Ross, S | + | [[Category: Ross, S A.]] |
| - | [[Category: Tezcan, F | + | [[Category: Tezcan, F A.]] |
| - | [[Category: Winkler, J | + | [[Category: Winkler, J R.]] |
[[Category: COH]] | [[Category: COH]] | ||
[[Category: cytochrome c]] | [[Category: cytochrome c]] | ||
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[[Category: intermediates]] | [[Category: intermediates]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:44:31 2008'' |
Revision as of 11:44, 21 February 2008
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CRYSTAL STRUCTURE OF COBALT(III)-SUBSTITUTED CYTOCHROME C (TUNA)
Overview
Replacement of iron with cobalt(III) selectively introduces a deep trap in the folding-energy landscape of the heme protein cytochrome c. Remarkably, neither the protein structure nor the folding thermodynamics is perturbed by this metal-ion substitution, as shown by data from spectroscopic and x-ray diffraction experiments. Through kinetics measurements, we have found parallel folding pathways involving several different misligated Co(III) species, and, as these folding intermediates persist for several hours under certain conditions, we have been able to elucidate fully their spectroscopic properties. The results, along with an analysis of the fluorescence energy-transfer kinetics during refolding, show that rapidly equilibrating populations of compact and extended polypeptide conformations are present until all molecules have reached the native structure. These measurements provide direct evidence that collapsed denatured structures are not substantially more stable than extended conformations of cytochrome c.
About this Structure
1LFM is a Single protein structure of sequence from Thunnus thynnus with as ligand. Full crystallographic information is available from OCA.
Reference
Using deeply trapped intermediates to map the cytochrome c folding landscape., Tezcan FA, Findley WM, Crane BR, Ross SA, Lyubovitsky JG, Gray HB, Winkler JR, Proc Natl Acad Sci U S A. 2002 Jun 25;99(13):8626-30. PMID:12084923
Page seeded by OCA on Thu Feb 21 13:44:31 2008
