Universität zu Köln

Wang, Jizong ORCID: 0000-0003-1085-5347, Wang, Jia ORCID: 0000-0002-5978-4191, Hu, Meijuan ORCID: 0000-0001-5326-0816, Wu, Shan ORCID: 0000-0002-4736-4755, Qi, Jinfeng ORCID: 0000-0002-4660-7495, Wang, Guoxun ORCID: 0000-0002-8033-5980, Han, Zhifu, Qi, Yijun, Gao, Ning ORCID: 0000-0003-3067-9993, Wang, Hong-Wei, Zhou, Jian-Min ORCID: 0000-0002-9943-2975 and Chai, Jijie (2019). Ligand-triggered allosteric ADP release primes a plant NLR complex. Science, 364 (6435). S. 43 - 81. WASHINGTON: AMER ASSOC ADVANCEMENT SCIENCE. ISSN 1095-9203

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Abstract

Pathogen recognition by nucleotide-binding (NB), leucine-rich repeat (LRR) receptors (NLRs) plays roles in plant immunity. The Xanthomonas campestris pv. campestris effector AvrAC uridylylates the Arabidopsis PBL2 kinase, and the latter (PBL2(UMP)) acts as a ligand to activate the NLR ZAR1 precomplexed with the RKS1 pseudokinase. Here we report the cryo-electron microscopy structures of ZAR1-RKS1 and ZAR1-RKS1-PBL2(UMP) in an inactive and intermediate state, respectively. The ZAR1(LRR) domain, compared with animal NLRLRR domains, is differently positioned to sequester ZAR1 in an inactive state. Recognition of PBL2(UMP) is exclusively through RKS1, which interacts with ZAR1(LRR). PBL2(UMP) binding stabilizes the RKS1 activation segment, which sterically blocks ZAR1 adenosine diphosphate (ADP) binding. This engenders a more flexible NB domain without conformational changes in the other ZAR1 domains. Our study provides a structural template for understanding plant NLRs.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Wang, Jizong UNSPECIFIED orcid.org/0000-0003-1085-5347 UNSPECIFIED Wang, Jia UNSPECIFIED orcid.org/0000-0002-5978-4191 UNSPECIFIED Hu, Meijuan UNSPECIFIED orcid.org/0000-0001-5326-0816 UNSPECIFIED Wu, Shan UNSPECIFIED orcid.org/0000-0002-4736-4755 UNSPECIFIED Qi, Jinfeng UNSPECIFIED orcid.org/0000-0002-4660-7495 UNSPECIFIED Wang, Guoxun UNSPECIFIED orcid.org/0000-0002-8033-5980 UNSPECIFIED Han, Zhifu UNSPECIFIED UNSPECIFIED UNSPECIFIED Qi, Yijun UNSPECIFIED UNSPECIFIED UNSPECIFIED Gao, Ning UNSPECIFIED orcid.org/0000-0003-3067-9993 UNSPECIFIED Wang, Hong-Wei UNSPECIFIED UNSPECIFIED UNSPECIFIED Zhou, Jian-Min UNSPECIFIED orcid.org/0000-0002-9943-2975 UNSPECIFIED Chai, Jijie UNSPECIFIED UNSPECIFIED UNSPECIFIED
URN:	urn:nbn:de:hbz:38-150944
DOI:	10.1126/science.aav5868
Journal or Publication Title:	Science
Volume:	364
Number:	6435
Page Range:	S. 43 - 81
Date:	2019
Publisher:	AMER ASSOC ADVANCEMENT SCIENCE
Place of Publication:	WASHINGTON
ISSN:	1095-9203
Language:	English
Faculty:	Faculty of Mathematics and Natural Sciences
Divisions:	Faculty of Mathematics and Natural Sciences > Department of Chemistry > Institute of Biochemistry
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language CRYO-EM STRUCTURE; RUST RESISTANCE PROTEIN; CRYSTAL-STRUCTURE; STRUCTURAL BASIS; RHO GTPASES; GENE; REVEALS; RECOGNITION; APOPTOSOME; EFFECTOR Multiple languages Multidisciplinary Sciences Multiple languages
Refereed:	Yes
URI:	http://kups.ub.uni-koeln.de/id/eprint/15094