6uh8
From Proteopedia
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<StructureSection load='6uh8' size='340' side='right'caption='[[6uh8]], [[Resolution|resolution]] 1.58Å' scene=''> | <StructureSection load='6uh8' size='340' side='right'caption='[[6uh8]], [[Resolution|resolution]] 1.58Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6uh8]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UH8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6UH8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6uh8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pethy Pethy]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UH8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6UH8 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dad2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4102 PETHY])</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=6uh8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uh8 OCA], [http://pdbe.org/6uh8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6uh8 RCSB], [http://www.ebi.ac.uk/pdbsum/6uh8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6uh8 ProSAT]</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=6uh8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uh8 OCA], [http://pdbe.org/6uh8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6uh8 RCSB], [http://www.ebi.ac.uk/pdbsum/6uh8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6uh8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| - | Strigolactones are | + | Strigolactones (SLs) are terpenoid-derived plant hormones that regulate various developmental processes, particularly shoot branching, root development, and leaf senescence. The SL receptor has an unusual mode of action. Upon binding SL, it hydrolyses the hormone, and then covalently binds one of the hydrolytic products. These initial events enable the SL receptor DAD2 (in petunia) to interact with the F-box protein PhMAX2A of the Skp-Cullin-F-box (SCF) complex and/or a repressor of SL signaling, PhD53A. However, it remains unclear how binding and hydrolysis structurally alters the SL receptor to enable its engagement with signaling partners. Here, we used mutagenesis to alter DAD2 and affect SL hydrolysis or DAD2's ability to interact with its signaling partners. We identified three DAD2 variants whose hydrolytic activity had been separated from the receptor's interactions with PhMAX2A or PhD53A. Two variants, DAD2(N242I) and DAD2(F135A), having substitutions in the core alpha/beta hydrolase fold domain and the hairpin, exhibited hormone-independent interactions with PhMAX2A and PhD53A respectively. Conversely, the DAD2(D166A) variant could not interact with PhMAX2A in the presence of SL, but its interaction with PhD53A remained unaffected. Structural analyses of DAD2N242I and DAD2D166A revealed only small differences compared with the structure of the wild-type receptor. Results of molecular dynamics simulations of the DAD2(N242I) structure suggested that increased flexibility is a likely cause for its SL-independent interaction with PhMAX2A. Our results suggest that PhMAX2A and PhD53A have distinct binding sites on the SL receptor and that its flexibility is a major determinant of its interactions with these two downstream regulators. |
| - | + | Flexibility of the petunia strigolactone receptor DAD2 promotes its interaction with signaling partners.,Lee HW, Sharma P, Janssen BJ, Drummond RSM, Luo Z, Hamiaux C, Collier T, Allison JR, Newcomb RD, Snowden KC J Biol Chem. 2020 Feb 17. pii: RA119.011509. doi: 10.1074/jbc.RA119.011509. PMID:32071083<ref>PMID:32071083</ref> | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Pethy]] | ||
[[Category: Hamiaux, C]] | [[Category: Hamiaux, C]] | ||
[[Category: Sharma, P]] | [[Category: Sharma, P]] | ||
Revision as of 07:21, 4 March 2020
Crystal structure of DAD2 N242I mutant
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