气候变化领域集成服务门户(CCPortal): Structural basis for a bacterial Pip system plant effector recognition protein

CCPortal

DOI	10.1073/pnas.2019462118
	Structural basis for a bacterial Pip system plant effector recognition protein
	Luo S.; Coutinho B.G.; Dadhwal P.; Oda Y.; Ren J.; Schaefer A.L.; Peter Greenberg E.; Harwood C.S.; Tong L.
发表日期	2021
ISSN	00278424
卷号	118 期号:10
英文摘要	A number of plant-associated proteobacteria have LuxR family transcription factors that we refer to as PipR subfamily members. PipR proteins play roles in interactions between bacteria and their plant hosts, and some are important for bacterial virulence of plants. We identified an ethanolamine derivative, N-(2-hydroxyethyl)-2-(2-hydroxyethylamino) acetamide (HEHEAA), as a potent effector of PipR-mediated gene regulation in the plant endophyte Pseudomonas GM79. HEHEAA-dependent PipR activity requires an ATP-binding cassette-type active transport system, and the periplasmic substrate-binding protein (SBP) of that system binds HEHEAA. To begin to understand the molecular basis of PipR system responses to plant factors we crystallized a HEHEAA-responsive SBP in the free- and HEHEAA-bound forms. The SBP, which is similar to peptide-binding SBPs, was in a closed conformation. A narrow cavity at the interface of its two lobes is wide enough to bind HEHEAA, but it cannot accommodate peptides with side chains. The polar atoms of HEHEAA are recognized by hydrogen-bonding interactions, and additional SBP residues contribute to the binding site. This binding mode was confirmed by a structure-based mutational analysis. We also show that a closely related SBP from the plant pathogen Pseudomonas syringae pv tomato DC3000 does not recognize HEHEAA. However, a single amino acid substitution in the presumed effector-binding pocket of the P. syringae SBP converted it to a weak HEHEAA-binding protein. The P. syringae PipR depends on a plant effector for activity, and our findings imply that different PipR-associated SBPs bind different effectors. © 2021 National Academy of Sciences. All rights reserved.
英文关键词	Populus; Pseudomonas signaling; Substrate-binding protein
语种	英语
scopus关键词	ABC transporter; ethanolamine derivative; transcription factor; transcription factor PipR; unclassified drug; Article; binding site; chemical binding; chemical interaction; controlled study; endophyte; gene control; gene mutation; hydrogen bond; nonhuman; priority journal; protein binding; protein conformation; protein structure; Pseudomonas syringae pv. tomato; signal transduction
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/180357
作者单位	Department of Biological Sciences, Columbia University, New York, NY 10027, United States; Department of Microbiology, University of Washington, Seattle, WA 98195, United States; Faculty of Biological Science and Technology, Changzhi University, Shanxi, 046011, China
推荐引用方式 GB/T 7714	Luo S.,Coutinho B.G.,Dadhwal P.,et al. Structural basis for a bacterial Pip system plant effector recognition protein[J],2021,118(10).
APA	Luo S..,Coutinho B.G..,Dadhwal P..,Oda Y..,Ren J..,...&Tong L..(2021).Structural basis for a bacterial Pip system plant effector recognition protein.Proceedings of the National Academy of Sciences of the United States of America,118(10).
MLA	Luo S.,et al."Structural basis for a bacterial Pip system plant effector recognition protein".Proceedings of the National Academy of Sciences of the United States of America 118.10(2021).