4B9H

Cladosporium fulvum LysM effector Ecp6 in complex with a beta-1,4- linked N-acetyl-D-glucosamine tetramer: I3C heavy atom derivative

4B9H の概要

• エントリーDOI: 10.2210/pdb4b9h/pdb
• 関連するPDBエントリー: 4B8V
• 分子名称: EXTRACELLULAR PROTEIN 6, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: sugar binding protein
• 由来する生物種: PASSALORA FULVA (TOMATO LEAF MOLD)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25927.35

構造登録者

Saleem-Batcha, R.,Sanchez-Vallet, A.,Hansen, G.,Thomma, B.P.H.J.,Mesters, J.R. (登録日: 2012-09-04, 公開日: 2013-07-17, 最終更新日: 2024-11-06)

主引用文献

Sanchez-Vallet, A.,Saleem-Batcha, R.,Kombrink, A.,Hansen, G.,Valkenburg, D.J.,Thomma, B.P.H.J.,Mesters, J.R.
Fungal Effector Ecp6 Outcompetes Host Immune Receptor for Chitin Binding Through Intrachain Lysm Dimerization
Elife, 2:00790-, 2013

PubMed Abstract: While host immune receptors detect pathogen-associated molecular patterns to activate immunity, pathogens attempt to deregulate host immunity through secreted effectors. Fungi employ LysM effectors to prevent recognition of cell wall-derived chitin by host immune receptors, although the mechanism to compete for chitin binding remained unclear. Structural analysis of the LysM effector Ecp6 of the fungal tomato pathogen Cladosporium fulvum reveals a novel mechanism for chitin binding, mediated by intrachain LysM dimerization, leading to a chitin-binding groove that is deeply buried in the effector protein. This composite binding site involves two of the three LysMs of Ecp6 and mediates chitin binding with ultra-high (pM) affinity. Intriguingly, the remaining singular LysM domain of Ecp6 binds chitin with low micromolar affinity but can nevertheless still perturb chitin-triggered immunity. Conceivably, the perturbation by this LysM domain is not established through chitin sequestration but possibly through interference with the host immune receptor complex. DOI:http://dx.doi.org/10.7554/eLife.00790.001.

PubMed: 23840930
DOI: 10.7554/ELIFE.00790

実験手法

X-RAY DIFFRACTION (2.1 Å)