1usz: 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 .. | 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== | ||
1USZ is a | 1USZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1USZ OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: upec]] | [[Category: upec]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:04:43 2007'' | ||
Revision as of 15:59, 5 November 2007
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SEMET AFAE-3 ADHESIN FROM ESCHERICHIA COLI
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
1USZ is a Single protein structure of sequence from Escherichia coli with SO4 and CL as ligands. Structure known Active Site: AC1. 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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