5oao
From Proteopedia
(Difference between revisions)
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<StructureSection load='5oao' size='340' side='right' caption='[[5oao]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='5oao' size='340' side='right' caption='[[5oao]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5oao]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OAO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OAO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5oao]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OAO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OAO FirstGlance]. <br> |
| - | </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=5oao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oao OCA], [http://pdbe.org/5oao PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oao RCSB], [http://www.ebi.ac.uk/pdbsum/5oao PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oao ProSAT]</span></td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RCD1, ATP8, CEO1, At1g32230, F3C3.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=5oao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oao OCA], [http://pdbe.org/5oao PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oao RCSB], [http://www.ebi.ac.uk/pdbsum/5oao PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oao ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/RCD1_ARATH RCD1_ARATH]] Inactive ADP-ribosyltransferase that functions with SRO1 to regulate oxidative stress, hormonal and developmental responses. Required for embryogenesis, vegetative and reproductive development, and abiotic stress responses. May regulate several stress-responsive genes. Seems to play a larger developmental role than SRO1. Does not bind NAD in vitro.<ref>PMID:11018516</ref> <ref>PMID:11041881</ref> <ref>PMID:14657410</ref> <ref>PMID:15208394</ref> <ref>PMID:15728341</ref> <ref>PMID:16926493</ref> <ref>PMID:19548978</ref> <ref>PMID:19625634</ref> <ref>PMID:20226034</ref> <ref>PMID:21172813</ref> | [[http://www.uniprot.org/uniprot/RCD1_ARATH RCD1_ARATH]] Inactive ADP-ribosyltransferase that functions with SRO1 to regulate oxidative stress, hormonal and developmental responses. Required for embryogenesis, vegetative and reproductive development, and abiotic stress responses. May regulate several stress-responsive genes. Seems to play a larger developmental role than SRO1. Does not bind NAD in vitro.<ref>PMID:11018516</ref> <ref>PMID:11041881</ref> <ref>PMID:14657410</ref> <ref>PMID:15208394</ref> <ref>PMID:15728341</ref> <ref>PMID:16926493</ref> <ref>PMID:19548978</ref> <ref>PMID:19625634</ref> <ref>PMID:20226034</ref> <ref>PMID:21172813</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Communication within cells relies on a few protein nodes called hubs, which organize vast interactomes with many partners. Frequently, hub proteins are intrinsically disordered conferring multi-specificity and dynamic communication. Conversely, folded hub proteins may organize networks using disordered partners. In this work, the structure of the RST domain, a unique folded hub, is solved by nuclear magnetic resonance spectroscopy and small-angle X-ray scattering, and its complex with a region of the transcription factor DREB2A is provided through data-driven HADDOCK modeling and mutagenesis analysis. The RST fold is unique, but similar structures are identified in the PAH (paired amphipathic helix), TAFH (TATA-box-associated factor homology), and NCBD (nuclear coactivator binding domain) domains. We designate them as a group the alphaalpha hubs, as they share an alphaalpha-hairpin super-secondary motif, which serves as an organizing platform for malleable helices of varying topology. This allows for partner adaptation, exclusion, and selection. Our findings provide valuable insights into structural features enabling signaling fidelity. | ||
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| + | Structure of Radical-Induced Cell Death1 Hub Domain Reveals a Common alphaalpha-Scaffold for Disorder in Transcriptional Networks.,Bugge K, Staby L, Kemplen KR, O'Shea C, Bendsen SK, Jensen MK, Olsen JG, Skriver K, Kragelund BB Structure. 2018 Apr 12. pii: S0969-2126(18)30094-7. doi:, 10.1016/j.str.2018.03.013. PMID:29657132<ref>PMID:29657132</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5oao" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Arath]] | ||
[[Category: Bugge, K]] | [[Category: Bugge, K]] | ||
[[Category: Kragelund, B B]] | [[Category: Kragelund, B B]] | ||
Revision as of 05:51, 25 April 2018
Solution structure of the complexed RCD1-RST
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