3ns2: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==High-resolution structure of pyrabactin-bound PYL2== | ==High-resolution structure of pyrabactin-bound PYL2== | ||
<StructureSection load='3ns2' size='340' side='right' caption='[[3ns2]], [[Resolution|resolution]] 1.63Å' scene=''> | <StructureSection load='3ns2' size='340' side='right'caption='[[3ns2]], [[Resolution|resolution]] 1.63Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3ns2]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NS2 OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[3ns2]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NS2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3NS2 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PYV:4-BROMO-N-(PYRIDIN-2-YLMETHYL)NAPHTHALENE-1-SULFONAMIDE'>PYV</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PYV:4-BROMO-N-(PYRIDIN-2-YLMETHYL)NAPHTHALENE-1-SULFONAMIDE'>PYV</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3kdh|3kdh]], [[3neg|3neg]], [[3nef|3nef]], [[3nr4|3nr4]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3kdh|3kdh]], [[3neg|3neg]], [[3nef|3nef]], [[3nr4|3nr4]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3ns2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ns2 OCA], [http://pdbe.org/3ns2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ns2 RCSB], [http://www.ebi.ac.uk/pdbsum/3ns2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ns2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| Line 31: | Line 31: | ||
==See Also== | ==See Also== | ||
*[[Abscisic acid receptor|Abscisic acid receptor]] | *[[Abscisic acid receptor 3D structures|Abscisic acid receptor 3D structures]] | ||
*[[PYR/PYL/RCAR family of ABA receptors|PYR/PYL/RCAR family of ABA receptors]] | *[[PYR/PYL/RCAR family of ABA receptors|PYR/PYL/RCAR family of ABA receptors]] | ||
== References == | == References == | ||
| Line 38: | Line 38: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Arath]] | [[Category: Arath]] | ||
[[Category: Large Structures]] | |||
[[Category: Hao, Q]] | [[Category: Hao, Q]] | ||
[[Category: Wang, J]] | [[Category: Wang, J]] | ||
Revision as of 11:07, 4 November 2020
High-resolution structure of pyrabactin-bound PYL2High-resolution structure of pyrabactin-bound PYL2
Structural highlights
Function[PYL2_ARATH] Receptor for abscisic acid (ABA) required for ABA-mediated responses such as stomatal closure and germination inhibition. Inhibits the activity of group-A protein phosphatases type 2C (PP2Cs) when activated by ABA.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAbscisic acid (ABA) is one of the most important phytohormones in plant. PYL proteins were identified to be ABA receptors in Arabidopsis thaliana. Despite the remarkably high degree of sequence similarity, PYL1 and PYL2 exhibit distinct responses toward pyrabactin, an ABA agonist. PYL1 inhibits protein phosphatase type 2C upon binding of pyrabactin. In contrast, PYL2 appears relatively insensitive to this compound. The crystal structure of pyrabactin-bound PYL1 revealed that most of the PYL1 residues involved in pyrabactin binding are conserved, hence failing to explain the selectivity of pyrabactin for PYL1 over PYL2. To understand the molecular basis of pyrabactin selectivity, we determined the crystal structure of PYL2 in complex with pyrabactin at 1.64 A resolution. Structural comparison and biochemical analyses demonstrated that one single amino acid alteration between a corresponding valine and isoleucine determines the distinct pyrabactin selectivity by PYL1 and PYL2. These characterizations provide an important clue to dissecting the redundancy of PYL proteins. Single Amino Acid Alteration between Valine and Isoleucine Determines the Distinct Pyrabactin Selectivity by PYL1 and PYL2.,Yuan X, Yin P, Hao Q, Yan C, Wang J, Yan N J Biol Chem. 2010 Sep 10;285(37):28953-8. Epub 2010 Jul 14. PMID:20630864[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||