1qxx: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1qxx.jpg|left|200px]] | [[Image:1qxx.jpg|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1qxx", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
--> | |||
{{STRUCTURE_1qxx| PDB=1qxx | SCENE= }} | |||
| | |||
}} | |||
'''CRYSTAL STRUCTURE OF THE C-TERMINAL DOMAIN OF TONB''' | '''CRYSTAL STRUCTURE OF THE C-TERMINAL DOMAIN OF TONB''' | ||
| Line 31: | Line 28: | ||
[[Category: Polzer, P.]] | [[Category: Polzer, P.]] | ||
[[Category: Welte, W.]] | [[Category: Welte, W.]] | ||
[[Category: | [[Category: Tonb dimerization]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:50:04 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 06:50, 3 May 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 Page seeded by OCA on Sat May 3 06:50:04 2008