1u07

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[[Image:1u07.gif|left|200px]]<br /><applet load="1u07" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1u07.gif|left|200px]]
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caption="1u07, resolution 1.13&Aring;" />
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'''Crystal Structure of the 92-residue C-term. part of TonB with significant structural changes compared to shorter fragments'''<br />
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{{Structure
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|PDB= 1u07 |SIZE=350|CAPTION= <scene name='initialview01'>1u07</scene>, resolution 1.13&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE= tonb ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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}}
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'''Crystal Structure of the 92-residue C-term. part of TonB with significant structural changes compared to shorter fragments'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1U07 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U07 OCA].
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1U07 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U07 OCA].
==Reference==
==Reference==
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Crystal structure of a 92-residue C-terminal fragment of TonB from Escherichia coli reveals significant conformational changes compared to structures of smaller TonB fragments., Kodding J, Killig F, Polzer P, Howard SP, Diederichs K, Welte W, J Biol Chem. 2005 Jan 28;280(4):3022-8. Epub 2004 Nov 2. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15522863 15522863]
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Crystal structure of a 92-residue C-terminal fragment of TonB from Escherichia coli reveals significant conformational changes compared to structures of smaller TonB fragments., Kodding J, Killig F, Polzer P, Howard SP, Diederichs K, Welte W, J Biol Chem. 2005 Jan 28;280(4):3022-8. Epub 2004 Nov 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15522863 15522863]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: beta-hairpin]]
[[Category: beta-hairpin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:19:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:25:34 2008''

Revision as of 12:25, 20 March 2008


PDB ID 1u07

Drag the structure with the mouse to rotate
, resolution 1.13Å
Gene: tonb (Escherichia coli)
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of the 92-residue C-term. part of TonB with significant structural changes compared to shorter fragments


Overview

Uptake of siderophores and vitamin B(12) through the outer membrane of Escherichia coli is effected by an active transport system consisting of several outer membrane receptors and a protein complex of the inner membrane. The link between these is TonB, a protein associated with the cytoplasmic membrane, which forms a large periplasmic domain capable of interacting with several outer membrane receptors, e.g. FhuA, FecA, and FepA for siderophores and BtuB for vitamin B(12.) The active transport across the outer membrane is driven by the chemiosmotic gradient of the inner membrane and is mediated by the TonB protein. The receptor-binding domain of TonB appears to be formed by a highly conserved C-terminal amino acid sequence of approximately 100 residues. Crystal structures of two C-terminal TonB fragments composed of 85 (TonB-85) and 77 (TonB-77) amino acid residues, respectively, have been previously determined (Chang, C., Mooser, A., Pluckthun, A., and Wlodawer, A. (2001) J. Biol. Chem. 276, 27535-27540 and Koedding, J., Howard, S. P., Kaufmann, L., Polzer, P., Lustig, A., and Welte, W. (2004) J. Biol. Chem. 279, 9978-9986). In both cases the TonB fragments form dimers in solution and crystallize as dimers consisting of monomers tightly engaged with one another by the exchange of a beta-hairpin and a C-terminal beta-strand. Here we present the crystal structure of a 92-residue fragment of TonB (TonB-92), which is monomeric in solution. The structure, determined at 1.13-A resolution, shows a dimer with considerably reduced intermolecular interaction compared with the other known TonB structures, in particular lacking the beta-hairpin exchange.

About this Structure

1U07 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of a 92-residue C-terminal fragment of TonB from Escherichia coli reveals significant conformational changes compared to structures of smaller TonB fragments., Kodding J, Killig F, Polzer P, Howard SP, Diederichs K, Welte W, J Biol Chem. 2005 Jan 28;280(4):3022-8. Epub 2004 Nov 2. PMID:15522863

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