6S2P

Structure of the NB-ARC domain from the Tomato immune receptor NRC1

Summary for 6S2P

• Entry DOI: 10.2210/pdb6s2p/pdb
• Descriptor: NRC1, ADENOSINE-5'-DIPHOSPHATE (2 entities in total)
• Functional Keywords: nlr receptor, nb-arc domain, plant immunity, plant protein
• Biological source: Solanum lycopersicum (Tomato)
• Total number of polymer chains: 1
• Total formula weight: 40578.38

Authors

Steele, J.F.C.,Banfield, M.J. (deposition date: 2019-06-21, release date: 2019-07-03, Last modification date: 2024-05-15)

Primary citation

Steele, J.F.C.,Hughes, R.K.,Banfield, M.J.
Structural and biochemical studies of an NB-ARC domain from a plant NLR immune receptor.
Plos One, 14:e0221226-e0221226, 2019

PubMed Abstract: Plant NLRs are modular immune receptors that trigger rapid cell death in response to attempted infection by pathogens. A highly conserved nucleotide-binding domain shared with APAF-1, various R-proteins and CED-4 (NB-ARC domain) is proposed to act as a molecular switch, cycling between ADP (repressed) and ATP (active) bound forms. Studies of plant NLR NB-ARC domains have revealed functional similarities to mammalian homologues, and provided insight into potential mechanisms of regulation. However, further advances have been limited by difficulties in obtaining sufficient yields of protein suitable for structural and biochemical techniques. From protein expression screens in Escherichia coli and Sf9 insect cells, we defined suitable conditions to produce the NB-ARC domain from the tomato NLR NRC1. Biophysical analyses of this domain showed it is a folded, soluble protein. Structural studies revealed the NRC1 NB-ARC domain had co-purified with ADP, and confirmed predicted structural similarities between plant NLR NB-ARC domains and their mammalian homologues.

PubMed: 31461469
DOI: 10.1371/journal.pone.0221226

Experimental method

X-RAY DIFFRACTION (2.5 Å)