1qgh

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[[Image:1qgh.gif|left|200px]]<br />
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[[Image:1qgh.gif|left|200px]]<br /><applet load="1qgh" size="450" color="white" frame="true" align="right" spinBox="true"
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<applet load="1qgh" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1qgh, resolution 2.35&Aring;" />
caption="1qgh, resolution 2.35&Aring;" />
'''THE X-RAY STRUCTURE OF THE UNUSUAL DODECAMERIC FERRITIN FROM LISTERIA INNOCUA, REVEALS A NOVEL INTERSUBUNIT IRON BINDING SITE.'''<br />
'''THE X-RAY STRUCTURE OF THE UNUSUAL DODECAMERIC FERRITIN FROM LISTERIA INNOCUA, REVEALS A NOVEL INTERSUBUNIT IRON BINDING SITE.'''<br />
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==About this Structure==
==About this Structure==
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1QGH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Listeria_innocua Listeria innocua] with FE as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Sites: ASA, ASB, ASC, ASD, ASE, ASF, ASG, ASH, ASI, ASJ, ASK and ASL. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QGH OCA].
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1QGH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Listeria_innocua Listeria innocua] with FE as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <scene name='pdbsite=ASA:Fe-Binding Site'>ASA</scene>, <scene name='pdbsite=ASB:Fe-Binding Site'>ASB</scene>, <scene name='pdbsite=ASC:Fe-Binding Site'>ASC</scene>, <scene name='pdbsite=ASD:Fe-Binding Site'>ASD</scene>, <scene name='pdbsite=ASE:Fe-Binding Site'>ASE</scene>, <scene name='pdbsite=ASF:Fe-Binding Site'>ASF</scene>, <scene name='pdbsite=ASG:Fe-Binding Site'>ASG</scene>, <scene name='pdbsite=ASH:Fe-Binding Site'>ASH</scene>, <scene name='pdbsite=ASI:Fe-Binding Site'>ASI</scene>, <scene name='pdbsite=ASJ:Fe-Binding Site'>ASJ</scene>, <scene name='pdbsite=ASK:Fe-Binding Site'>ASK</scene> and <scene name='pdbsite=ASL:Fe-Binding Site'>ASL</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QGH OCA].
==Reference==
==Reference==
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[[Category: ferritin]]
[[Category: ferritin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 16:59:45 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 17:52:18 2007''

Revision as of 15:42, 18 December 2007


1qgh, resolution 2.35Å

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THE X-RAY STRUCTURE OF THE UNUSUAL DODECAMERIC FERRITIN FROM LISTERIA INNOCUA, REVEALS A NOVEL INTERSUBUNIT IRON BINDING SITE.

Overview

Ferritin is characterized by a highly conserved architecture that, comprises 24 subunits assembled into a spherical cage with 432 symmetry., The only known exception is the dodecameric ferritin from Listeria, innocua. The structure of Listeria ferritin has been determined to a, resolution of 2.35 A by molecular replacement, using as a search model the, structure of Dps from Escherichia coli. The Listeria 12-mer is endowed, with 23 symmetry and displays the functionally relevant structural, features of the ferritin 24-mer, namely the negatively charged channels, along the three-fold symmetry axes that serve for iron entry into the, cavity and a negatively charged internal cavity for iron deposition. The, electron density map shows 12 iron ions on the inner surface of the hollow, core, at the interface between monomers related by two-fold axes. Analysis, of the nature and stereochemistry of the iron-binding ligands reveals, strong similarities with known ferroxidase sites. The L. innocua ferritin, site, however, is the first described so far that has ligands belonging to, two different subunits and is not contained within a four-helix bundle.

About this Structure

1QGH is a Single protein structure of sequence from Listeria innocua with FE as ligand. Known structural/functional Sites: , , , , , , , , , , and . Full crystallographic information is available from OCA.

Reference

The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site., Ilari A, Stefanini S, Chiancone E, Tsernoglou D, Nat Struct Biol. 2000 Jan;7(1):38-43. PMID:10625425

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