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1BF8

PERIPLASMIC CHAPERONE FIMC, NMR, 20 STRUCTURES

1BF8 の概要
エントリーDOI10.2210/pdb1bf8/pdb
分子名称CHAPERONE PROTEIN FIMC (1 entity in total)
機能のキーワードchaperone, fimc, periplasmic chaperone, pilus chaperone, type-i pili
由来する生物種Escherichia coli
タンパク質・核酸の鎖数1
化学式量合計22754.03
構造登録者
Pellecchia, M.,Guntert, P.,Glockshuber, R.,Wuthrich, K. (登録日: 1998-05-28, 公開日: 1998-11-18, 最終更新日: 2024-05-22)
主引用文献Pellecchia, M.,Guntert, P.,Glockshuber, R.,Wuthrich, K.
NMR solution structure of the periplasmic chaperone FimC.
Nat.Struct.Biol., 5:885-890, 1998
Cited by
PubMed Abstract: The NMR structure of the 205-residue periplasmic chaperone FimC is presented. This protein consists of two globular domains with immunoglobulin-like folds connected by a 15-residue linker peptide. The relative orientation of the two domains is defined by hydrophobic contacts and an interdomain salt bridge. FimC mediates the assembly of type-1 pili, which are filamentous surface organelles of uropathogenic Escherichia coli strains that enable the bacteria to attach to host cell surfaces and persist in macrophages. The availability of the NMR structure of FimC provides a new basis for rational design of drugs against infections by uropathogenic bacteria.
PubMed: 9783748
DOI: 10.1038/2325
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 1bf8
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2024-10-30に公開中

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