Structural basis for a bacterial Pip system plant effector recognition protein
| العنوان: | Structural basis for a bacterial Pip system plant effector recognition protein |
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| المؤلفون: | Shukun Luo, Liang Tong, Bruna G. Coutinho, Amy L. Schaefer, Jiahong Ren, Prikshat Dadhwal, E. Peter Greenberg, Caroline S. Harwood, Yasuhiro Oda |
| المصدر: | Proc Natl Acad Sci U S A |
| بيانات النشر: | Proceedings of the National Academy of Sciences, 2021. |
| سنة النشر: | 2021 |
| مصطلحات موضوعية: | Regulation of gene expression, Binding Sites, Multidisciplinary, Subfamily, biology, Effector, Chemistry, Pseudomonas, Pseudomonas syringae, Periplasmic space, Biological Sciences, Crystallography, X-Ray, biology.organism_classification, Bacterial Proteins, Biochemistry, Acetamides, Binding site, Transcription factor |
| الوصف: | 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. |
| تدمد: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.2019462118 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0363691b82417a637ff083d92bbee8da https://doi.org/10.1073/pnas.2019462118 |
| Rights: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....0363691b82417a637ff083d92bbee8da |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 10916490 00278424 |
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| DOI: | 10.1073/pnas.2019462118 |