1UT1
DraE adhesin from Escherichia Coli
1UT1 の概要
エントリーDOI | 10.2210/pdb1ut1/pdb |
関連するPDBエントリー | 1USQ 1USZ 1UT2 |
分子名称 | DR HEMAGGLUTININ STRUCTURAL SUBUNIT, SULFATE ION, 1,2-ETHANEDIOL, ... (4 entities in total) |
機能のキーワード | adhesin, protein binding fimbrial adhesin, upec, daec, protein binding |
由来する生物種 | ESCHERICHIA COLI |
細胞内の位置 | Fimbrium: P24093 |
タンパク質・核酸の鎖数 | 6 |
化学式量合計 | 99511.39 |
構造登録者 | Anderson, K.L.,Billington, J.,Pettigrew, D.,Cota, E.,Roversi, P.,Simpson, P.,Chen, H.A.,Urvil, P.,Dumerle, L.,Barlow, P.,Medof, E.,Smith, R.A.G.,Nowicki, B.,Le Bouguenec, C.,Lea, S.M.,Matthews, S. (登録日: 2003-12-02, 公開日: 2004-08-31, 最終更新日: 2024-11-20) |
主引用文献 | Pettigrew, D.,Anderson, K.L.,Billington, J.,Cota, E.,Simpson, P.,Urvil, P.,Rabuzin, F.,Roversi, P.,Nowicki, B.,Du Merle, L.,Le Bouguenec, C.,Matthews, S.,Lea, S.M. High Resolution Studies of the Afa/Dr Adhesin Drae and its Interaction with Chloramphenicol J.Biol.Chem., 279:46851-, 2004 Cited by PubMed Abstract: 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. PubMed: 15331605DOI: 10.1074/JBC.M409284200 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.7 Å) |
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