1ihr: Difference between revisions

Revision as of 12:13, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1ihr.png

Template:STRUCTURE 1ihr

Crystal structure of the dimeric C-terminal domain of TonBCrystal structure of the dimeric C-terminal domain of TonB

Template:ABSTRACT PUBMED 11328822

About this StructureAbout this Structure

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

ReferenceReference

Crystal structure of the dimeric C-terminal domain of TonB reveals a novel fold., Chang C, Mooser A, Pluckthun A, Wlodawer A, J Biol Chem. 2001 Jul 20;276(29):27535-40. Epub 2001 Apr 27. PMID:11328822

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OCA

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-[[Image:1ihr.gif|left|200px]]
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-'''Crystal structure of the dimeric C-terminal domain of TonB'''
+===Crystal structure of the dimeric C-terminal domain of TonB===
-==Overview==
+<!--
-The TonB-dependent complex of Gram-negative bacteria couples the inner membrane proton motive force to the active transport of iron.siderophore and vitamin B(12) across the outer membrane. The structural basis of that process has not been described so far in full detail. The crystal structure of the C-terminal domain of TonB from Escherichia coli has now been solved by multiwavelength anomalous diffraction and refined at 1.55-A resolution, providing the first evidence that this region of TonB (residues 164-239) dimerizes. Moreover, the structure shows a novel architecture that has no structural homologs among any known proteins. The dimer of the C-terminal domain of TonB is cylinder-shaped with a length of 65 A and a diameter of 25 A. Each monomer contains three beta strands and a single alpha helix. The two monomers are intertwined with each other, and all six beta-strands of the dimer make a large antiparallel beta-sheet. We propose a plausible model of binding of TonB to FhuA and FepA, two TonB-dependent outer-membrane receptors.
+The line below this paragraph, {{ABSTRACT_PUBMED_11328822}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11328822 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_11328822}}
 ==About this Structure==
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 [[Category: Intertwined dimer]]
 [[Category: Novel fold]]
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