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1USQ

Complex of E. Coli DraE adhesin with Chloramphenicol

1USQ の概要
エントリーDOI10.2210/pdb1usq/pdb
関連するPDBエントリー1UT1
分子名称DR HEMAGGLUTININ STRUCTURAL SUBUNIT, SULFATE ION, 1,2-ETHANEDIOL, ... (5 entities in total)
機能のキーワードadhesin, drae, fimbrial adhesin, chloramphenicol, upec, daec
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100985.47
構造登録者
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: 15331605
DOI: 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 (1.9 Å)
構造検証レポート
Validation report summary of 1usq
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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