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


2grx, resolution 3.300Å

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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

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