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| [[Image:1ujw.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1ujw| PDB=1ujw | SCENE= }} | | {{STRUCTURE_1ujw| PDB=1ujw | SCENE= }} |
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| '''Structure of the complex between BtuB and Colicin E3 Receptor binding domain'''
| | ===Structure of the complex between BtuB and Colicin E3 Receptor binding domain=== |
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| ==Overview==
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| Cellular import of colicin E3 is initiated by the Escherichia coli outer membrane cobalamin transporter, BtuB. The 135-residue 100-A coiled-coil receptor-binding domain (R135) of colicin E3 forms a 1:1 complex with BtuB whose structure at a resolution of 2.75 A is reported. Binding of R135 to the BtuB extracellular surface (DeltaG(o) = -12 kcal mol(-1)) is mediated by 27 residues of R135 near the coiled-coil apex. Formation of the R135-BtuB complex results in unfolding of R135 N- and C-terminal ends, inferred to be important for unfolding of the colicin T-domain. Small conformational changes occur in the BtuB cork and barrel domains but are insufficient to form a translocation channel. The absence of a channel and the peripheral binding of R135 imply that BtuB serves to bind the colicin, and that the coiled-coil delivers the colicin to a neighboring outer membrane protein for translocation, thus forming a colicin translocon. The translocator was concluded to be OmpF from the occlusion of OmpF channels by colicin E3.
| | The line below this paragraph, {{ABSTRACT_PUBMED_14528295}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 14528295 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_14528295}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Beta-barrel]] | | [[Category: Beta-barrel]] |
| [[Category: Coiled-coil]] | | [[Category: Coiled-coil]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:19:35 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:50:06 2008'' |
