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5TOS

Botrytis-induced kinase 1 (BIK1) from Arabidopsis thaliana

Summary for 5TOS
Entry DOI10.2210/pdb5tos/pdb
DescriptorSerine/threonine-protein kinase BIK1 (2 entities in total)
Functional Keywordsserine/threonine-protein kinase, bik1, pamp-triggered immunity, transferase
Biological sourceArabidopsis thaliana (Mouse-ear cress)
Total number of polymer chains2
Total formula weight88478.84
Authors
Hurlburt, N.K.,Lal, N.K.,Fisher, A.J. (deposition date: 2016-10-18, release date: 2018-04-18, Last modification date: 2024-11-20)
Primary citationLal, N.K.,Nagalakshmi, U.,Hurlburt, N.K.,Flores, R.,Bak, A.,Sone, P.,Ma, X.,Song, G.,Walley, J.,Shan, L.,He, P.,Casteel, C.,Fisher, A.J.,Dinesh-Kumar, S.P.
The Receptor-like Cytoplasmic Kinase BIK1 Localizes to the Nucleus and Regulates Defense Hormone Expression during Plant Innate Immunity.
Cell Host Microbe, 23:485-497.e5, 2018
Cited by
PubMed Abstract: Plants employ cell-surface pattern recognition receptors (PRRs) to detect pathogens. Although phytohormones produced during PRR signaling play an essential role in innate immunity, a direct link between PRR activation and hormone regulation is unknown. EFR is a PRR that recognizes bacterial EF-Tu and activates immune signaling. Here we report that EFR regulates the phytohormone jasmonic acid (JA) through direct phosphorylation of a receptor-like cytoplasmic kinase, BIK1. The BIK1 structure revealed that the EFR-phosphorylated sites reside on a uniquely extended loop away from the BIK1 kinase core domain. Phosphomimetic mutations of these sites resulted in increased phytohormones and enhanced resistance to bacterial infections. In addition to its documented plasma membrane localization, BIK1 also localizes to the nucleus and interacts directly with WRKY transcription factors involved in the JA and salicylic acid (SA) regulation. These findings demonstrate the mechanistic basis of signal transduction from PRR to phytohormones, mediated through a PRR-BIK1-WRKY axis.
PubMed: 29649442
DOI: 10.1016/j.chom.2018.03.010
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.35 Å)
Structure validation

237735

数据于2025-06-18公开中

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