1soy
From Proteopedia
(New page: 200px<br /><applet load="1soy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1soy" /> '''Solution structure of the bacterial frataxin...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1soy.jpg|left|200px]]<br /><applet load="1soy" size=" | + | [[Image:1soy.jpg|left|200px]]<br /><applet load="1soy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1soy" /> | caption="1soy" /> | ||
'''Solution structure of the bacterial frataxin orthologue, CyaY'''<br /> | '''Solution structure of the bacterial frataxin orthologue, CyaY'''<br /> | ||
==Overview== | ==Overview== | ||
| - | CyaY is the bacterial ortholog of frataxin, a small mitochondrial iron | + | CyaY is the bacterial ortholog of frataxin, a small mitochondrial iron binding protein thought to be involved in iron sulphur cluster formation. Loss of frataxin function leads to the neurodegenerative disorder Friedreich's ataxia. We have solved the solution structure of CyaY and used the structural information to map iron binding onto the protein surface. Comparison of the behavior of wild-type CyaY with that of a mutant indicates that specific binding with a defined stoichiometry does not require aggregation and that the main binding site, which hosts both Fe(2+) and Fe(3+), occupies a highly anionic surface of the molecule. This function is conserved across species since the corresponding region of human frataxin is also able to bind iron, albeit with weaker affinity. The presence of secondary binding sites on CyaY, but not on frataxin, hints at a possible polymerization mechanism. We suggest mutations that may provide further insights into the frataxin function. |
==About this Structure== | ==About this Structure== | ||
| - | 1SOY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1SOY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SOY OCA]. |
==Reference== | ==Reference== | ||
| Line 23: | Line 23: | ||
[[Category: nmr]] | [[Category: nmr]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:03:47 2008'' |
Revision as of 13:03, 21 February 2008
|
Solution structure of the bacterial frataxin orthologue, CyaY
Overview
CyaY is the bacterial ortholog of frataxin, a small mitochondrial iron binding protein thought to be involved in iron sulphur cluster formation. Loss of frataxin function leads to the neurodegenerative disorder Friedreich's ataxia. We have solved the solution structure of CyaY and used the structural information to map iron binding onto the protein surface. Comparison of the behavior of wild-type CyaY with that of a mutant indicates that specific binding with a defined stoichiometry does not require aggregation and that the main binding site, which hosts both Fe(2+) and Fe(3+), occupies a highly anionic surface of the molecule. This function is conserved across species since the corresponding region of human frataxin is also able to bind iron, albeit with weaker affinity. The presence of secondary binding sites on CyaY, but not on frataxin, hints at a possible polymerization mechanism. We suggest mutations that may provide further insights into the frataxin function.
About this Structure
1SOY is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Solution structure of the bacterial frataxin ortholog, CyaY: mapping the iron binding sites., Nair M, Adinolfi S, Pastore C, Kelly G, Temussi P, Pastore A, Structure. 2004 Nov;12(11):2037-48. PMID:15530368
Page seeded by OCA on Thu Feb 21 15:03:47 2008
