3QFL

Coiled-Coil Domain-Dependent Homodimerization of Intracellular MLA Immune Receptors Defines a Minimal Functional Module for Triggering Cell Death

Summary for 3QFL

• Entry DOI: 10.2210/pdb3qfl/pdb
• Descriptor: MLA10 (2 entities in total)
• Functional Keywords: coiled-coil, (cc) domain, nlrs, nucleotide-binding domain, leucine-rich repeat containing receptors, protein binding
• Biological source: Hordeum vulgare (barley)
• Total number of polymer chains: 1
• Total formula weight: 13154.91

Authors

Chai, J.,Cheng, W. (deposition date: 2011-01-21, release date: 2011-05-04, Last modification date: 2024-10-30)

Primary citation

Maekawa, T.,Cheng, W.,Spiridon, L.N.,Toller, A.,Lukasik, E.,Saijo, Y.,Liu, P.,Shen, Q.H.,Micluta, M.A.,Somssich, I.E.,Takken, F.L.,Petrescu, A.J.,Chai, J.,Schulze-Lefert, P.
Coiled-Coil Domain-Dependent Homodimerization of Intracellular Barley Immune Receptors Defines a Minimal Functional Module for Triggering Cell Death
Cell Host Microbe, 9:187-199, 2011

PubMed Abstract: Plants and animals have evolved structurally related innate immune sensors, designated NLRs, to detect intracellular nonself molecules. NLRs are modular, consisting of N-terminal coiled-coil (CC) or TOLL/interleukin-1 receptor (TIR) domains, a central nucleotide-binding (NB) domain, and C-terminal leucine-rich repeats (LRRs). The polymorphic barley mildew A (MLA) locus encodes CC-containing allelic immune receptors recognizing effectors of the pathogenic powdery mildew fungus. We report the crystal structure of an MLA receptor's invariant CC domain, which reveals a rod-shaped homodimer. MLA receptors also self-associate in vivo, but self-association appears to be independent of effector-triggered receptor activation. MLA CC mutants that fail to self-interact impair in planta cell death activity triggered by the CC domain alone and by an autoactive full-length MLA receptor that mimics its ATP-bound state. Thus, CC domain-dependent dimerization of the immune sensor defines a minimal functional unit and implies a role for the dimeric CC module in downstream immune signaling.

PubMed: 21402358
DOI: 10.1016/j.chom.2011.02.008

Experimental method

X-RAY DIFFRACTION (1.997 Å)