2ga5
From Proteopedia
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[[Image:2ga5.gif|left|200px]] | [[Image:2ga5.gif|left|200px]] | ||
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'''yeast frataxin''' | '''yeast frataxin''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2GA5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. This structure supersedes the now removed PDB entry | + | 2GA5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1xaq 1xaq]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GA5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Proteasa, S V.]] | [[Category: Proteasa, S V.]] | ||
[[Category: Zhang, Y.]] | [[Category: Zhang, Y.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:52:32 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 01:52, 4 May 2008
yeast frataxin
Overview
The mitochondrial protein frataxin is essential for cellular regulation of iron homeostasis. Although the exact function of frataxin is not yet clear, recent reports indicate the protein binds iron and can act as a mitochondrial iron chaperone to transport Fe(II) to ferrochelatase and ISU proteins within the heme and iron-sulfur cluster biosynthetic pathways, respectively. We have determined the solution structure of apo yeast frataxin to provide a structural basis of how frataxin binds and donates iron to the ferrochelatase. While the protein's alpha-beta-sandwich structural motif is similar to that observed for human and bacterial frataxins, the yeast structure presented in this report includes the full N-terminus observed for the mature processed protein found within the mitochondrion. In addition, NMR spectroscopy was used to identify frataxin amino acids that are perturbed by the presence of iron. Conserved acidic residues in the helix 1-strand 1 protein region undergo amide chemical shift changes in the presence of Fe(II), indicating a possible iron-binding site on frataxin. NMR spectroscopy was further used to identify the intermolecular binding interface between ferrochelatase and frataxin. Ferrochelatase appears to bind to frataxin's helical plane in a manner that includes its iron-binding interface.
About this Structure
2GA5 is a Single protein structure of sequence from Saccharomyces cerevisiae. This structure supersedes the now removed PDB entry 1xaq. Full crystallographic information is available from OCA.
Reference
Yeast frataxin solution structure, iron binding, and ferrochelatase interaction., He Y, Alam SL, Proteasa SV, Zhang Y, Lesuisse E, Dancis A, Stemmler TL, Biochemistry. 2004 Dec 28;43(51):16254-62. PMID:15610019 Page seeded by OCA on Sun May 4 04:52:32 2008
