1by5

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(New page: 200px<br /><applet load="1by5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1by5, resolution 2.60&Aring;" /> '''FHUA FROM E. COLI, W...)
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[[Image:1by5.jpg|left|200px]]<br /><applet load="1by5" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1by5.jpg|left|200px]]<br /><applet load="1by5" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1by5, resolution 2.60&Aring;" />
caption="1by5, resolution 2.60&Aring;" />
'''FHUA FROM E. COLI, WITH ITS LIGAND FERRICHROME'''<br />
'''FHUA FROM E. COLI, WITH ITS LIGAND FERRICHROME'''<br />
==Overview==
==Overview==
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FhuA protein facilitates ligand-gated transport of ferrichrome-bound iron, across Escherichia coli outer membranes. X-ray analysis at 2.7 A, resolution reveals two distinct conformations in the presence and absence, of ferrichrome. The monomeric protein consists of a hollow, 22-stranded, antiparallel beta barrel (residues 160-714), which is obstructed by a plug, (residues 19-159). The binding site of ferrichrome, an aromatic pocket, near the cell surface, undergoes minor changes upon association with the, ligand. These are propagated and amplified across the plug, eventually, resulting in substantially different protein conformations at the, periplasmic face. Our findings reveal the mechanism of signal transmission, and suggest how the energy-transducing TonB complex senses ligand binding.
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FhuA protein facilitates ligand-gated transport of ferrichrome-bound iron across Escherichia coli outer membranes. X-ray analysis at 2.7 A resolution reveals two distinct conformations in the presence and absence of ferrichrome. The monomeric protein consists of a hollow, 22-stranded, antiparallel beta barrel (residues 160-714), which is obstructed by a plug (residues 19-159). The binding site of ferrichrome, an aromatic pocket near the cell surface, undergoes minor changes upon association with the ligand. These are propagated and amplified across the plug, eventually resulting in substantially different protein conformations at the periplasmic face. Our findings reveal the mechanism of signal transmission and suggest how the energy-transducing TonB complex senses ligand binding.
==About this Structure==
==About this Structure==
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1BY5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Ustilago_sphaerogena Ustilago sphaerogena] with FE and OES as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BY5 OCA].
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1BY5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Ustilago_sphaerogena Ustilago sphaerogena] with <scene name='pdbligand=FE:'>FE</scene> and <scene name='pdbligand=OES:'>OES</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BY5 OCA].
==Reference==
==Reference==
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[[Category: Ustilago sphaerogena]]
[[Category: Ustilago sphaerogena]]
[[Category: Koebnik, R.]]
[[Category: Koebnik, R.]]
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[[Category: Locher, K.P.]]
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[[Category: Locher, K P.]]
[[Category: Mitschler, A.]]
[[Category: Mitschler, A.]]
[[Category: Moras, D.]]
[[Category: Moras, D.]]
[[Category: Moulinier, L.]]
[[Category: Moulinier, L.]]
[[Category: Rees, B.]]
[[Category: Rees, B.]]
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[[Category: Rosenbusch, J.P.]]
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[[Category: Rosenbusch, J P.]]
[[Category: FE]]
[[Category: FE]]
[[Category: OES]]
[[Category: OES]]
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[[Category: membrane protein]]
[[Category: membrane protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:01:04 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:00:23 2008''

Revision as of 10:00, 21 February 2008


1by5, resolution 2.60Å

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FHUA FROM E. COLI, WITH ITS LIGAND FERRICHROME

Overview

FhuA protein facilitates ligand-gated transport of ferrichrome-bound iron across Escherichia coli outer membranes. X-ray analysis at 2.7 A resolution reveals two distinct conformations in the presence and absence of ferrichrome. The monomeric protein consists of a hollow, 22-stranded, antiparallel beta barrel (residues 160-714), which is obstructed by a plug (residues 19-159). The binding site of ferrichrome, an aromatic pocket near the cell surface, undergoes minor changes upon association with the ligand. These are propagated and amplified across the plug, eventually resulting in substantially different protein conformations at the periplasmic face. Our findings reveal the mechanism of signal transmission and suggest how the energy-transducing TonB complex senses ligand binding.

About this Structure

1BY5 is a Single protein structure of sequence from Escherichia coli and Ustilago sphaerogena with and as ligands. Full crystallographic information is available from OCA.

Reference

Transmembrane signaling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal allosteric changes., Locher KP, Rees B, Koebnik R, Mitschler A, Moulinier L, Rosenbusch JP, Moras D, Cell. 1998 Dec 11;95(6):771-8. PMID:9865695

Page seeded by OCA on Thu Feb 21 12:00:23 2008

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