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6k87
From Proteopedia
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==The closed state of RGLG1 VWA domain with MIDAS is occupied by water== | ==The closed state of RGLG1 VWA domain with MIDAS is occupied by water== | ||
| - | <StructureSection load='6k87' size='340' side='right'caption='[[6k87]]' scene=''> | + | <StructureSection load='6k87' size='340' side='right'caption='[[6k87]], [[Resolution|resolution]] 1.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K87 OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6k87]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K87 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6K87 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.502Å</td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6k87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k87 OCA], [https://pdbe.org/6k87 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6k87 RCSB], [https://www.ebi.ac.uk/pdbsum/6k87 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6k87 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/RGLG1_ARATH RGLG1_ARATH] E3 ubiquitin-protein ligase that mediates the formation of 'Lys-63'-linked ubiquitin chains. Regulates apical dominance by acting on the auxin transport proteins abundance (PubMed:17586653). Together with RGLG5, mediates the ubiquitination and subsequent proteasomal degradation of the target protein PP2CA. Functions as positive regulator of abscisic acid (ABA) signaling through ABA-dependent degradation of PP2CA, a major inhibitor of ABA signaling (PubMed:27577789). Acts as a negative regulator of drought stress response (PubMed:22095047).<ref>PMID:17586653</ref> <ref>PMID:22095047</ref> <ref>PMID:27577789</ref> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Arabidopsis thaliana]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Wang Q]] | [[Category: Wang Q]] | ||
[[Category: Wu Y]] | [[Category: Wu Y]] | ||
Current revision
The closed state of RGLG1 VWA domain with MIDAS is occupied by water
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