1qxx: Difference between revisions

Revision as of 15:44, 21 February 2008

CRYSTAL STRUCTURE OF THE C-TERMINAL DOMAIN OF TONB

OverviewOverview

FhuA belongs to a family of specific siderophore transport systems located in the outer membrane of Escherichia coli. The energy required for the transport process is provided by the proton motive force of the cytoplasmic membrane and is transmitted to FhuA by the protein TonB. Although the structure of full-length TonB is not known, the structure of the last 77 residues of a fragment composed of the 86 C-terminal amino acids was recently solved and shows an intertwined dimer (Chang, C., Mooser, A., Pluckthun, A., and Wlodawer, A. (2001) J. Biol. Chem. 276, 27535-27540). We analyzed the ability of truncated C-terminal TonB fragments of different lengths (77, 86, 96, 106, 116, and 126 amino acid residues, respectively) to bind to the receptor FhuA. Only the shortest TonB fragment, TonB-77, could not effectively interact with FhuA. We have also observed that the fragments TonB-77 and TonB-86 form homodimers in solution, whereas the longer fragments remain monomeric. TonB fragments that bind to FhuA in vitro also inhibit ferrichrome uptake via FhuA in vivo and protect cells against attack by bacteriophage Phi80.

About this StructureAbout this Structure

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

ReferenceReference

Dimerization of TonB is not essential for its binding to the outer membrane siderophore receptor FhuA of Escherichia coli., Koedding J, Howard P, Kaufmann L, Polzer P, Lustig A, Welte W, J Biol Chem. 2004 Mar 12;279(11):9978-86. Epub 2003 Dec 8. PMID:14665631

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OCA

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-[[Image:1qxx.jpg|left|200px]]<br /><applet load="1qxx" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="1qxx, resolution 2.7&Aring;" />
 '''CRYSTAL STRUCTURE OF THE C-TERMINAL DOMAIN OF TONB'''<br />
 ==Overview==
-FhuA belongs to a family of specific siderophore transport systems located, in the outer membrane of Escherichia coli. The energy required for the, transport process is provided by the proton motive force of the, cytoplasmic membrane and is transmitted to FhuA by the protein TonB., Although the structure of full-length TonB is not known, the structure of, the last 77 residues of a fragment composed of the 86 C-terminal amino, acids was recently solved and shows an intertwined dimer (Chang, C., Mooser, A., Pluckthun, A., and Wlodawer, A. (2001) J. Biol. Chem. 276, 27535-27540). We analyzed the ability of truncated C-terminal TonB, fragments of different lengths (77, 86, 96, 106, 116, and 126 amino acid, residues, respectively) to bind to the receptor FhuA. Only the shortest, TonB fragment, TonB-77, could not effectively interact with FhuA. We have, also observed that the fragments TonB-77 and TonB-86 form homodimers in, solution, whereas the longer fragments remain monomeric. TonB fragments, that bind to FhuA in vitro also inhibit ferrichrome uptake via FhuA in, vivo and protect cells against attack by bacteriophage Phi80.
+FhuA belongs to a family of specific siderophore transport systems located in the outer membrane of Escherichia coli. The energy required for the transport process is provided by the proton motive force of the cytoplasmic membrane and is transmitted to FhuA by the protein TonB. Although the structure of full-length TonB is not known, the structure of the last 77 residues of a fragment composed of the 86 C-terminal amino acids was recently solved and shows an intertwined dimer (Chang, C., Mooser, A., Pluckthun, A., and Wlodawer, A. (2001) J. Biol. Chem. 276, 27535-27540). We analyzed the ability of truncated C-terminal TonB fragments of different lengths (77, 86, 96, 106, 116, and 126 amino acid residues, respectively) to bind to the receptor FhuA. Only the shortest TonB fragment, TonB-77, could not effectively interact with FhuA. We have also observed that the fragments TonB-77 and TonB-86 form homodimers in solution, whereas the longer fragments remain monomeric. TonB fragments that bind to FhuA in vitro also inhibit ferrichrome uptake via FhuA in vivo and protect cells against attack by bacteriophage Phi80.
 ==About this Structure==
-QXX 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QXX OCA].
+QXX 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=1QXX OCA].
 ==Reference==
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 [[Category: tonb dimerization]]
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