1usq: Difference between revisions

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==Overview==
==Overview==
Pathogenic Escherichia coli expressing Afa/Dr adhesins are able to cause, both urinary tract and diarrheal infections. The Afa/Dr adhesins confer, adherence to epithelial cells via interactions with the human complement, regulating protein, decay accelerating factor (DAF or CD55). Two of the, Afa/Dr adhesions, AfaE-III and DraE, differ from each other by only three, residues but are reported to have several different properties. One such, difference is disruption of the interaction between DraE and CD55 by, chloramphenicol, whereas binding of AfaE-III to CD55 is unaffected. Here, we present a crystal structure of a strand-swapped trimer of wild type, DraE. We also present a crystal structure of this trimer in complex with, chloramphenicol, as well as NMR data supporting the binding position of, chloramphenicol within the crystal. The crystal structure reveals the, precise atomic basis for the sensitivity of DraE-CD55 binding to, chloramphenicol and demonstrates that in contrast to other, chloramphenicol-protein complexes, drug binding is mediated via, recognition of the chlorine "tail" rather than via intercalation of the, benzene rings into a hydrophobic pocket.
Pathogenic Escherichia coli expressing Afa/Dr adhesins are able to cause both urinary tract and diarrheal infections. The Afa/Dr adhesins confer adherence to epithelial cells via interactions with the human complement regulating protein, decay accelerating factor (DAF or CD55). Two of the Afa/Dr adhesions, AfaE-III and DraE, differ from each other by only three residues but are reported to have several different properties. One such difference is disruption of the interaction between DraE and CD55 by chloramphenicol, whereas binding of AfaE-III to CD55 is unaffected. Here we present a crystal structure of a strand-swapped trimer of wild type DraE. We also present a crystal structure of this trimer in complex with chloramphenicol, as well as NMR data supporting the binding position of chloramphenicol within the crystal. The crystal structure reveals the precise atomic basis for the sensitivity of DraE-CD55 binding to chloramphenicol and demonstrates that in contrast to other chloramphenicol-protein complexes, drug binding is mediated via recognition of the chlorine "tail" rather than via intercalation of the benzene rings into a hydrophobic pocket.


==About this Structure==
==About this Structure==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Anderson, K.L.]]
[[Category: Anderson, K L.]]
[[Category: Barlow, P.]]
[[Category: Barlow, P.]]
[[Category: Billington, J.]]
[[Category: Billington, J.]]
[[Category: Bouguenec, C.Le.]]
[[Category: Bouguenec, C Le.]]
[[Category: Chen, H.A.]]
[[Category: Chen, H A.]]
[[Category: Cota, E.]]
[[Category: Cota, E.]]
[[Category: Dumerle, L.]]
[[Category: Dumerle, L.]]
[[Category: Lea, S.M.]]
[[Category: Lea, S M.]]
[[Category: Matthews, S.]]
[[Category: Matthews, S.]]
[[Category: Medof, E.]]
[[Category: Medof, E.]]
Line 27: Line 27:
[[Category: Roversi, P.]]
[[Category: Roversi, P.]]
[[Category: Simpson, P.]]
[[Category: Simpson, P.]]
[[Category: Smith, R.A.G.]]
[[Category: Smith, R A.G.]]
[[Category: Urvil, P.]]
[[Category: Urvil, P.]]
[[Category: CLM]]
[[Category: CLM]]
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[[Category: upec]]
[[Category: upec]]


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Revision as of 16:27, 21 February 2008

File:1usq.gif


1usq, resolution 1.9Å

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COMPLEX OF E. COLI DRAE ADHESIN WITH CHLORAMPHENICOL

OverviewOverview

Pathogenic Escherichia coli expressing Afa/Dr adhesins are able to cause both urinary tract and diarrheal infections. The Afa/Dr adhesins confer adherence to epithelial cells via interactions with the human complement regulating protein, decay accelerating factor (DAF or CD55). Two of the Afa/Dr adhesions, AfaE-III and DraE, differ from each other by only three residues but are reported to have several different properties. One such difference is disruption of the interaction between DraE and CD55 by chloramphenicol, whereas binding of AfaE-III to CD55 is unaffected. Here we present a crystal structure of a strand-swapped trimer of wild type DraE. We also present a crystal structure of this trimer in complex with chloramphenicol, as well as NMR data supporting the binding position of chloramphenicol within the crystal. The crystal structure reveals the precise atomic basis for the sensitivity of DraE-CD55 binding to chloramphenicol and demonstrates that in contrast to other chloramphenicol-protein complexes, drug binding is mediated via recognition of the chlorine "tail" rather than via intercalation of the benzene rings into a hydrophobic pocket.

About this StructureAbout this Structure

1USQ is a Single protein structure of sequence from Escherichia coli with , and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

ReferenceReference

High resolution studies of the Afa/Dr adhesin DraE and its interaction with chloramphenicol., Pettigrew D, Anderson KL, Billington J, Cota E, Simpson P, Urvil P, Rabuzin F, Roversi P, Nowicki B, du Merle L, Le Bouguenec C, Matthews S, Lea SM, J Biol Chem. 2004 Nov 5;279(45):46851-7. Epub 2004 Aug 24. PMID:15331605

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