1ut1
From Proteopedia
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|PDB= 1ut1 |SIZE=350|CAPTION= <scene name='initialview01'>1ut1</scene>, resolution 1.7Å | |PDB= 1ut1 |SIZE=350|CAPTION= <scene name='initialview01'>1ut1</scene>, resolution 1.7Å | ||
|SITE= <scene name='pdbsite=AC1:Egl+Binding+Site+For+Chain+F'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Egl+Binding+Site+For+Chain+F'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ut1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ut1 OCA], [http://www.ebi.ac.uk/pdbsum/1ut1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ut1 RCSB]</span> | ||
}} | }} | ||
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[[Category: Smith, R A.G.]] | [[Category: Smith, R A.G.]] | ||
[[Category: Urvil, P.]] | [[Category: Urvil, P.]] | ||
| - | [[Category: EDO]] | ||
| - | [[Category: SO4]] | ||
[[Category: daec]] | [[Category: daec]] | ||
[[Category: drae]] | [[Category: drae]] | ||
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[[Category: upec]] | [[Category: upec]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:14:49 2008'' |
Revision as of 21:14, 30 March 2008
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| , resolution 1.7Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
DRAE ADHESIN FROM ESCHERICHIA COLI
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.
About this Structure
1UT1 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Mar 31 00:14:49 2008
Categories: Escherichia coli | Single protein | Anderson, K L. | Barlow, P. | Billington, J. | Bouguenec, C Le. | Chen, H A. | Cota, E. | Dumerle, L. | Lea, S M. | Matthews, S. | Medof, E. | Nowicki, B. | Pettigrew, D. | Roversi, P. | Simpson, P. | Smith, R A.G. | Urvil, P. | Daec | Drae | Fimbrial adhesin | Upec
