5dnu
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Striga KAI2-like protein in complex with karrikin== | |
| + | <StructureSection load='5dnu' size='340' side='right' caption='[[5dnu]], [[Resolution|resolution]] 1.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5dnu]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DNU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DNU FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BEZ:BENZOIC+ACID'>BEZ</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=KKN:3-METHYL-2H-FURO[2,3-C]PYRAN-2-ONE'>KKN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dnv|5dnv]], [[5dnw|5dnw]]</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=5dnu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dnu OCA], [http://pdbe.org/5dnu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dnu RCSB], [http://www.ebi.ac.uk/pdbsum/5dnu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dnu ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The perception of two plant germination inducers, karrikins and strigolactones, are mediated by the proteins KAI2 and D14. Recently, KAI2-type proteins from parasitic weeds, which are possibly related to seed germination induced by strigolactone, have been classified into three clades characterized by different responses to karrikin/strigolactone. Here we characterized a karrikin-binding protein in Striga (ShKAI2iB) that belongs to intermediate-evolving KAI2 and provided the structural bases for its karrikin-binding specificity. Binding assays showed that ShKAI2iB bound karrikins but not strigolactone, differing from other KAI2 and D14. The crystal structures of ShKAI2iB and ShKAI2iB-karrikin complex revealed obvious structural differences in a helix located at the entry of its ligand-binding cavity. This results in a smaller closed pocket, which is also the major cause of ShKAI2iB's specificity of binding karrikin. Our structural study also revealed that a few non-conserved amino acids led to the distinct ligand-binding profile of ShKAI2iB, suggesting that the evolution of KAI2 resulted in its diverse functions. | ||
| - | + | Structural basis of unique ligand specificity of KAI2-like protein from parasitic weed Striga hermonthica.,Xu Y, Miyakawa T, Nakamura H, Nakamura A, Imamura Y, Asami T, Tanokura M Sci Rep. 2016 Aug 10;6:31386. doi: 10.1038/srep31386. PMID:27507097<ref>PMID:27507097</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5dnu" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Miyakawa, T]] | ||
| + | [[Category: Nakamura, A]] | ||
| + | [[Category: Tanokura, M]] | ||
| + | [[Category: Xu, Y]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Kai2 karrikin striga]] | ||
Revision as of 05:21, 9 September 2016
Crystal structure of Striga KAI2-like protein in complex with karrikin
| |||||||||||
