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1S21

Crystal Structure of AvrPphF ORF2, A Type III Effector from P. syringae

1S21 の概要
エントリーDOI10.2210/pdb1s21/pdb
分子名称ORF2 (2 entities in total)
機能のキーワードpredominantly beta-strand, chaperone
由来する生物種Pseudomonas syringae pv. phaseolicola
タンパク質・核酸の鎖数1
化学式量合計22050.24
構造登録者
Singer, A.U.,Desveaux, D.,Betts, L.,Chang, J.H.,Nimchuk, Z.,Grant, S.R.,Dangl, J.K.,Sondek, J. (登録日: 2004-01-07, 公開日: 2004-09-14, 最終更新日: 2024-02-14)
主引用文献Singer, A.U.,Desveaux, D.,Betts, L.,Chang, J.H.,Nimchuk, Z.,Grant, S.R.,Dangl, J.K.,Sondek, J.
Crystal Structures of the Type III Effector Protein AvrPphF and Its Chaperone Reveal Residues Required for Plant Pathogenesis
Structure, 12:1669-1681, 2004
Cited by
PubMed Abstract: The avrPphF locus from Pseudomonas syringae pv. phaseolicola, the causative agent of bean halo-blight disease, encodes proteins which either enhance virulence on susceptible hosts or elicit defense responses on hosts carrying the R1 resistance gene. Here we present the crystal structures of the two proteins from the avrPphF operon. The structure of AvrPphF ORF1 is strikingly reminiscent of type III chaperones from bacterial pathogens of animals, indicating structural conservation of these specialized chaperones, despite high sequence divergence. The AvrPphF ORF2 effector adopts a novel "mushroom"-like structure containing "head" and "stalk" subdomains. The head subdomain possesses limited structural homology to the catalytic domain of bacterial ADP-ribosyltransferases (ADP-RTs), though no ADP-RT activity was detected for AvrPphF ORF2 in standard assays. Nonetheless, this structural similarity identified two clusters of conserved surface-exposed residues important for both virulence mediated by AvrPphF ORF2 and recognition of this effector by bean plants expressing the R1 resistance gene.
PubMed: 15341731
DOI: 10.1016/j.str.2004.06.023
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2 Å)
構造検証レポート
Validation report summary of 1s21
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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