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| | <StructureSection load='5e02' size='340' side='right'caption='[[5e02]], [[Resolution|resolution]] 3.80Å' scene=''> | | <StructureSection load='5e02' size='340' side='right'caption='[[5e02]], [[Resolution|resolution]] 3.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5e02]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chrysonilia_crassa Chrysonilia crassa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E02 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E02 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5e02]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Neurospora_crassa Neurospora crassa] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E02 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E02 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dzr|5dzr]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">B9B11.040, frh, NCU03363.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5141 Chrysonilia crassa])</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=5e02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e02 OCA], [https://pdbe.org/5e02 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e02 RCSB], [https://www.ebi.ac.uk/pdbsum/5e02 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e02 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=5e02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e02 OCA], [http://pdbe.org/5e02 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e02 RCSB], [http://www.ebi.ac.uk/pdbsum/5e02 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e02 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q1K502_NEUCR Q1K502_NEUCR] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chrysonilia crassa]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Conrad, K S]] | + | [[Category: Neurospora crassa]] |
| - | [[Category: Crane, B C]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Circadian clock]] | + | [[Category: Conrad KS]] |
| - | [[Category: Hydrolase]] | + | [[Category: Crane BC]] |
| - | [[Category: Rna binding protein-rna complex]]
| + | |
| Structural highlights
Function
Q1K502_NEUCR
Publication Abstract from PubMed
In the Neurospora crassa circadian clock, a protein complex of frequency (FRQ), casein kinase 1a (CK1a), and the FRQ-interacting RNA Helicase (FRH) rhythmically represses gene expression by the white-collar complex (WCC). FRH crystal structures in several conformations and bound to ADP/RNA reveal differences between FRH and the yeast homolog Mtr4 that clarify the distinct role of FRH in the clock. The FRQ-interacting region at the FRH N-terminus has variable structure in the absence of FRQ A known mutation that disrupts circadian rhythms (R806H) resides in a positively charged surface of the KOW domain, far removed from the helicase core. We show that changes to other similarly located residues modulate interactions with the WCC and FRQ A V142G substitution near the N-terminus also alters FRQ and WCC binding to FRH, but produces an unusual short clock period. These data support the assertion that FRH helicase activity does not play an essential role in the clock, but rather FRH acts to mediate contacts among FRQ, CK1a and the WCC through interactions involving its N-terminus and KOW module.
Structure of the frequency-interacting RNA helicase: a protein interaction hub for the circadian clock.,Conrad KS, Hurley JM, Widom J, Ringelberg CS, Loros JJ, Dunlap JC, Crane BR EMBO J. 2016 Jun 23. pii: e201694327. PMID:27340124[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Conrad KS, Hurley JM, Widom J, Ringelberg CS, Loros JJ, Dunlap JC, Crane BR. Structure of the frequency-interacting RNA helicase: a protein interaction hub for the circadian clock. EMBO J. 2016 Jun 23. pii: e201694327. PMID:27340124 doi:http://dx.doi.org/10.15252/embj.201694327
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