1xx3

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[[Image:1xx3.gif|left|200px]]
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{{Structure
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|GENE= tonB, exbA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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{{STRUCTURE_1xx3| PDB=1xx3 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xx3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xx3 OCA], [http://www.ebi.ac.uk/pdbsum/1xx3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xx3 RCSB]</span>
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'''Solution Structure of Escherichia coli TonB-CTD'''
'''Solution Structure of Escherichia coli TonB-CTD'''
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[[Category: Vogel, H J.]]
[[Category: Vogel, H J.]]
[[Category: Weljie, A M.]]
[[Category: Weljie, A M.]]
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[[Category: c-terminal domain]]
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[[Category: C-terminal domain]]
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[[Category: nmr]]
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[[Category: Nmr]]
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[[Category: tonb-ctd]]
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[[Category: Tonb-ctd]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:37:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:55:49 2008''
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Revision as of 12:37, 3 May 2008

Template:STRUCTURE 1xx3

Solution Structure of Escherichia coli TonB-CTD


Overview

The TonB protein transduces energy from the proton gradient across the cytoplasmic membrane of Gram-negative bacteria to TonB-dependent outer membrane receptors. It is a critically important protein in iron uptake, and deletion of this protein is known to decrease virulence of bacteria in animal models. This system has been used for Trojan horse antibiotic delivery. Here, we describe the high-resolution solution structure of Escherichia coli TonB residues 103-239 (TonB-CTD). TonB-CTD is monomeric with an unstructured N terminus (103-151) and a well structured C terminus (152-239). The structure contains a four-stranded antiparallel beta-sheet packed against two alpha-helices and an extended strand in a configuration homologous to the C-terminal domain of the TolA protein. Chemical shift perturbations to the TonB-CTD (1)H-(15)N HSCQ spectrum titrated with TonB box peptides modeled from the E.coli FhuA, FepA and BtuB proteins were all equivalent, indicating that all three peptides bind to the same region of TonB. Isothermal titration calorimetry measurements demonstrate that TonB-CTD interacts with the FhuA-derived peptide with a K(D)=36(+/-7) microM. On the basis of chemical shift data, the position of Gln160, and comparison to the TolA gp3 N1 complex crystal structure, we propose that the TonB box binds to TonB-CTD along the beta3-strand.

About this Structure

1XX3 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The solution structure of the C-terminal domain of TonB and interaction studies with TonB box peptides., Sean Peacock R, Weljie AM, Peter Howard S, Price FD, Vogel HJ, J Mol Biol. 2005 Feb 4;345(5):1185-97. Epub 2004 Dec 15. PMID:15644214 Page seeded by OCA on Sat May 3 15:37:00 2008

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