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1KDL

Solution structure of the amphipathic domain of YopD from Yersinia

1KDL の概要
エントリーDOI10.2210/pdb1kdl/pdb
分子名称YOPD protein (1 entity in total)
機能のキーワードyersinia, yopd, amphipathic alpha helix, beta turn, structural protein
タンパク質・核酸の鎖数1
化学式量合計2768.20
構造登録者
Tengel, T.,Sethson, I.,Francis, M.S. (登録日: 2001-11-13, 公開日: 2002-08-21, 最終更新日: 2024-05-01)
主引用文献Tengel, T.,Sethson, I.,Francis, M.S.
Conformational analysis by CD and NMR spectroscopy of a peptide encompassing the amphipathic domain of YopD from Yersinia.
Eur.J.Biochem., 269:3659-3668, 2002
Cited by
PubMed Abstract: To establish an infection, Yersinia pseudotuberculosis utilizes a plasmid-encoded type III secretion machine that permits the translocation of several anti-host factors into the cytosol of target eukaryotic cells. Secreted YopD is essential for this process. Pre-secretory stabilization of YopD is mediated by an interaction with its cognate chaperone, LcrH. YopD possesses LcrH binding domains located in the N-terminus and in a predicted amphipathic domain located near the C-terminus. This latter domain is also critical for Yersinia virulence. In this study, we designed synthetic peptides encompassing the C-terminal amphipathic domain of YopD. A solution structure of YopD278-300, a peptide that strongly interacted with LcrH, was obtained by NMR methods. The structure is composed of a well-defined amphipathic alpha helix ranging from Phe280 to Tyr291, followed by a type I beta turn between residues Val292 and His295. The C-terminal truncated peptides, YopD278-292 and YopD271-292, lacked helical structure, implicating the beta turn in helix stability. An interaction between YopD278-300 and its cognate chaperone, LcrH, was observed by NMR through line-broadening effects and chemical shift differences between the free peptide and the peptide-LcrH complex. These effects were not observed for the unstructured peptide, YopD278-292, which confirms that the alpha helical structure of the YopD amphipathic domain is a critical binding region of LcrH.
PubMed: 12153562
DOI: 10.1046/j.1432-1033.2002.03051.x
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 1kdl
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2026-04-22に公開中

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