4eyv
From Proteopedia
(Difference between revisions)
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| - | + | ==Crystal structure of Cyclophilin A like protein from Piriformospora indica== | |
| - | + | <StructureSection load='4eyv' size='340' side='right' caption='[[4eyv]], [[Resolution|resolution]] 1.97Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4eyv]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Piriformospora_indica Piriformospora indica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EYV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EYV FirstGlance]. <br> | |
| - | ==Function== | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4eyv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eyv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4eyv RCSB], [http://www.ebi.ac.uk/pdbsum/4eyv PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
[[http://www.uniprot.org/uniprot/C6KGV3_PIRIN C6KGV3_PIRIN]] PPIases accelerate the folding of proteins (By similarity).[RuleBase:RU000493] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).[RuleBase:RU004223] | [[http://www.uniprot.org/uniprot/C6KGV3_PIRIN C6KGV3_PIRIN]] PPIases accelerate the folding of proteins (By similarity).[RuleBase:RU000493] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).[RuleBase:RU004223] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | Structure of RNA-interacting Cyclophilin A-like protein from Piriformospora indica that provides salinity-stress tolerance in plants.,Trivedi DK, Bhatt H, Pal RK, Tuteja R, Garg B, Johri AK, Bhavesh NS, Tuteja N Sci Rep. 2013 Oct 21;3:3001. doi: 10.1038/srep03001. PMID:24141523<ref>PMID:24141523</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
[[Category: Piriformospora indica]] | [[Category: Piriformospora indica]] | ||
| - | [[Category: Bhatt, H | + | [[Category: Bhatt, H]] |
| - | [[Category: Bhavesh, N S | + | [[Category: Bhavesh, N S]] |
| - | [[Category: Pal, R K | + | [[Category: Pal, R K]] |
| - | [[Category: Tuteja, N | + | [[Category: Tuteja, N]] |
[[Category: Cyclophilin motif]] | [[Category: Cyclophilin motif]] | ||
[[Category: Fungus]] | [[Category: Fungus]] | ||
[[Category: Isomerase]] | [[Category: Isomerase]] | ||
[[Category: Salt tolerance]] | [[Category: Salt tolerance]] | ||
Revision as of 02:31, 25 December 2014
Crystal structure of Cyclophilin A like protein from Piriformospora indica
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