4EYV

Crystal structure of Cyclophilin A like protein from Piriformospora indica

Summary for 4EYV

• Entry DOI: 10.2210/pdb4eyv/pdb
• Descriptor: Peptidyl-prolyl cis-trans isomerase, POTASSIUM ION, SODIUM ION, ... (5 entities in total)
• Functional Keywords: cyclophilin motif, fungus, salt tolerance, isomerase
• Biological source: Piriformospora indica
• Total number of polymer chains: 3
• Total formula weight: 54905.68

Authors

Bhatt, H.,Pal, R.K.,Tuteja, N.,Bhavesh, N.S. (deposition date: 2012-05-02, release date: 2013-05-15, Last modification date: 2023-11-08)

Primary citation

Trivedi, D.K.,Bhatt, H.,Pal, R.K.,Tuteja, R.,Garg, B.,Johri, A.K.,Bhavesh, N.S.,Tuteja, N.
Structure of RNA-interacting Cyclophilin A-like protein from Piriformospora indica that provides salinity-stress tolerance in plants
Sci Rep, 3:3001-3001, 2013

PubMed Abstract: Soil salinity problems are widespread around the globe with increased risk of spreading over the years. The fungus Piriformospora indica, identified in Indian Thar desert, colonizes the roots of monocotyledon plants and provides resistance towards biotic as well as abiotic stress conditions. We have identified a cyclophilin A-like protein from P. indica (PiCypA), which shows higher expression levels during salinity stress. The transgenic tobacco plants overexpressing PiCypA develop osmotic tolerance and exhibit normal growth under osmotic stress conditions. The crystal structure and NMR spectroscopy of PiCypA show a canonical cyclophilin like fold exhibiting a novel RNA binding activity. The RNA binding activity of the protein and identification of the key residues involved in the RNA recognition is unique for this class of protein. Here, we demonstrate for the first time a direct evidence of countering osmotic stress tolerance in plant by genetic modification using a P. indica gene.

PubMed: 24141523
DOI: 10.1038/srep03001

Experimental method

X-RAY DIFFRACTION (1.97 Å)