2cjn
From Proteopedia
(New page: 200px<br /><applet load="2cjn" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cjn" /> '''STRUCTURE OF FERREDOXIN, NMR, MINIMIZED AVER...) |
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| - | [[Image:2cjn.gif|left|200px]]<br /><applet load="2cjn" size=" | + | [[Image:2cjn.gif|left|200px]]<br /><applet load="2cjn" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2cjn" /> | caption="2cjn" /> | ||
'''STRUCTURE OF FERREDOXIN, NMR, MINIMIZED AVERAGE STRUCTURE'''<br /> | '''STRUCTURE OF FERREDOXIN, NMR, MINIMIZED AVERAGE STRUCTURE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of ferredoxin, purified from the | + | The three-dimensional structure of ferredoxin, purified from the thermophilic cyanobacterium Synechococcus elongatus, was determined in aqueous solution by two-dimensional proton nuclear magnetic resonance. In addition to the 946 distance constraints from nuclear Overhauser effect connectivities, we added 241 distance constraints derived from the crystal structure of Spirulina platensis ferredoxin to the 19 residues close to the [2Fe-2S] iron-sulfur center, where crosspeaks disappeared due to paramagnetic effects. The atomic root-mean-square difference of the ten converged structures from the mean structure was 0.61(+/-0.12) A for backbone atoms (N, C(alpha), C'). The main-chain structure was almost the same as the crystal structures of other mesophile ferredoxins, but comparison of the side-chain structures revealed an extension of the hydrophobic core, a unique hydrophobic patch on the surface of the large beta-sheet, and two unique charge networks in this thermostable ferredoxin structure, some of which might contribute to thermostability. |
==About this Structure== | ==About this Structure== | ||
| - | 2CJN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synechococcus_elongatus Synechococcus elongatus]. This structure | + | 2CJN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synechococcus_elongatus Synechococcus elongatus]. This structure supersedes the now removed PDB entry 1CJN. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CJN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: iron-sulfur protein]] | [[Category: iron-sulfur protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:49:21 2008'' |
Revision as of 14:49, 21 February 2008
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STRUCTURE OF FERREDOXIN, NMR, MINIMIZED AVERAGE STRUCTURE
Overview
The three-dimensional structure of ferredoxin, purified from the thermophilic cyanobacterium Synechococcus elongatus, was determined in aqueous solution by two-dimensional proton nuclear magnetic resonance. In addition to the 946 distance constraints from nuclear Overhauser effect connectivities, we added 241 distance constraints derived from the crystal structure of Spirulina platensis ferredoxin to the 19 residues close to the [2Fe-2S] iron-sulfur center, where crosspeaks disappeared due to paramagnetic effects. The atomic root-mean-square difference of the ten converged structures from the mean structure was 0.61(+/-0.12) A for backbone atoms (N, C(alpha), C'). The main-chain structure was almost the same as the crystal structures of other mesophile ferredoxins, but comparison of the side-chain structures revealed an extension of the hydrophobic core, a unique hydrophobic patch on the surface of the large beta-sheet, and two unique charge networks in this thermostable ferredoxin structure, some of which might contribute to thermostability.
About this Structure
2CJN is a Single protein structure of sequence from Synechococcus elongatus. This structure supersedes the now removed PDB entry 1CJN. Full crystallographic information is available from OCA.
Reference
Solution structure of ferredoxin from the thermophilic cyanobacterium Synechococcus elongatus and its thermostability., Hatanaka H, Tanimura R, Katoh S, Inagaki F, J Mol Biol. 1997 May 23;268(5):922-33. PMID:9180381
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