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2grx

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(New page: 200px<br /><applet load="2grx" size="450" color="white" frame="true" align="right" spinBox="true" caption="2grx, resolution 3.300&Aring;" /> '''Crystal structure o...)
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[[Image:2grx.gif|left|200px]]<br /><applet load="2grx" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2grx.gif|left|200px]]<br /><applet load="2grx" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2grx, resolution 3.300&Aring;" />
caption="2grx, resolution 3.300&Aring;" />
'''Crystal structure of TonB in complex with FhuA, E. coli outer membrane receptor for ferrichrome'''<br />
'''Crystal structure of TonB in complex with FhuA, E. coli outer membrane receptor for ferrichrome'''<br />
==Overview==
==Overview==
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The cytoplasmic membrane protein TonB spans the periplasm of the, Gram-negative bacterial cell envelope, contacts cognate outer membrane, receptors, and facilitates siderophore transport. The outer membrane, receptor FhuA from Escherichia coli mediates TonB-dependent import of, ferrichrome. We report the 3.3 angstrom resolution crystal structure of, the TonB carboxyl-terminal domain in complex with FhuA. TonB contacts, stabilize FhuA's amino-terminal residues, including those of the consensus, Ton box sequence that form an interprotein beta sheet with TonB through, strand exchange. The highly conserved TonB residue arginine-166 is, oriented to form multiple contacts with the FhuA cork, the globular domain, enclosed by the beta barrel.
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The cytoplasmic membrane protein TonB spans the periplasm of the Gram-negative bacterial cell envelope, contacts cognate outer membrane receptors, and facilitates siderophore transport. The outer membrane receptor FhuA from Escherichia coli mediates TonB-dependent import of ferrichrome. We report the 3.3 angstrom resolution crystal structure of the TonB carboxyl-terminal domain in complex with FhuA. TonB contacts stabilize FhuA's amino-terminal residues, including those of the consensus Ton box sequence that form an interprotein beta sheet with TonB through strand exchange. The highly conserved TonB residue arginine-166 is oriented to form multiple contacts with the FhuA cork, the globular domain enclosed by the beta barrel.
==About this Structure==
==About this Structure==
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2GRX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PO4, FTT, DPO, DAO, MYR, EAP and FCI as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2GRX OCA].
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2GRX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=FTT:'>FTT</scene>, <scene name='pdbligand=DPO:'>DPO</scene>, <scene name='pdbligand=DAO:'>DAO</scene>, <scene name='pdbligand=MYR:'>MYR</scene>, <scene name='pdbligand=EAP:'>EAP</scene> and <scene name='pdbligand=FCI:'>FCI</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GRX OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Allaire, M.]]
[[Category: Allaire, M.]]
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[[Category: Coulton, J.W.]]
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[[Category: Coulton, J W.]]
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[[Category: Pawelek, P.D.]]
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[[Category: Pawelek, P D.]]
[[Category: DAO]]
[[Category: DAO]]
[[Category: DPO]]
[[Category: DPO]]
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[[Category: protein-protein]]
[[Category: protein-protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:21:42 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:34:40 2008''

Revision as of 15:34, 21 February 2008

Image:2grx.gif

2grx, resolution 3.300Å

Drag the structure with the mouse to rotate

Crystal structure of TonB in complex with FhuA, E. coli outer membrane receptor for ferrichrome

Overview

The cytoplasmic membrane protein TonB spans the periplasm of the Gram-negative bacterial cell envelope, contacts cognate outer membrane receptors, and facilitates siderophore transport. The outer membrane receptor FhuA from Escherichia coli mediates TonB-dependent import of ferrichrome. We report the 3.3 angstrom resolution crystal structure of the TonB carboxyl-terminal domain in complex with FhuA. TonB contacts stabilize FhuA's amino-terminal residues, including those of the consensus Ton box sequence that form an interprotein beta sheet with TonB through strand exchange. The highly conserved TonB residue arginine-166 is oriented to form multiple contacts with the FhuA cork, the globular domain enclosed by the beta barrel.

About this Structure

2GRX is a Protein complex structure of sequences from Escherichia coli with , , , , , and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of TonB in complex with FhuA, E. coli outer membrane receptor., Pawelek PD, Croteau N, Ng-Thow-Hing C, Khursigara CM, Moiseeva N, Allaire M, Coulton JW, Science. 2006 Jun 2;312(5778):1399-402. PMID:16741125

Page seeded by OCA on Thu Feb 21 17:34:40 2008

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