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| | ==NMR structure of Xenopus RecQ4 zinc knuckle== | | ==NMR structure of Xenopus RecQ4 zinc knuckle== |
| - | <StructureSection load='2mpj' size='340' side='right' caption='[[2mpj]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | + | <StructureSection load='2mpj' size='340' side='right'caption='[[2mpj]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2mpj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/African_clawed_frog African clawed frog]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MPJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MPJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2mpj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MPJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MPJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RTS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 African clawed frog])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=2mpj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mpj OCA], [http://pdbe.org/2mpj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mpj RCSB], [http://www.ebi.ac.uk/pdbsum/2mpj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2mpj ProSAT]</span></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=2mpj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mpj OCA], [https://pdbe.org/2mpj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mpj RCSB], [https://www.ebi.ac.uk/pdbsum/2mpj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mpj ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/B1WBC8_XENLA B1WBC8_XENLA] |
| | <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: African clawed frog]] | + | [[Category: Large Structures]] |
| - | [[Category: Marino, F]] | + | [[Category: Xenopus laevis]] |
| - | [[Category: Mojumdar, A]] | + | [[Category: Marino F]] |
| - | [[Category: Musco, G]] | + | [[Category: Mojumdar A]] |
| - | [[Category: Onesti, S]] | + | [[Category: Musco G]] |
| - | [[Category: Zucchelli, C]] | + | [[Category: Onesti S]] |
| - | [[Category: Dna/rna binding]]
| + | [[Category: Zucchelli C]] |
| - | [[Category: Helicase]]
| + | |
| - | [[Category: Nucleotide binding protein]]
| + | |
| - | [[Category: Protein]]
| + | |
| - | [[Category: Recq4]]
| + | |
| - | [[Category: Zinc knuckle]]
| + | |
| Structural highlights
Function
B1WBC8_XENLA
Publication Abstract from PubMed
The RecQ4 helicase belongs to the ubiquitous RecQ family but its exact role in the cell is not completely understood. In addition to the helicase domain, RecQ4 has a unique N-terminal part that is essential for viability and is constituted by a region homologous to the yeast Sld2 replication initiation factor, followed by a cysteine-rich region, predicted to fold as a Zn knuckle. We carried out a structural and biochemical analysis of both the human and Xenopus laevis RecQ4 cysteine-rich regions, and showed by NMR spectroscopy that the Xenopus fragment indeed assumes the canonical Zn knuckle fold, whereas the human sequence remains unstructured, consistent with the mutation of one of the Zn ligands. Both the human and Xenopus Zn knuckles bind to a variety of nucleic acid substrates, with a mild preference for RNA. We also investigated the effect of a segment located upstream the Zn knuckle that is highly conserved and rich in positively charged and aromatic residues, partially overlapping with the C-terminus of the Sld2-like domain. In both the human and Xenopus proteins, the presence of this region strongly enhances binding to nucleic acids. These results reveal novel possible roles of RecQ4 in DNA replication and genome stability.
Structural and biochemical characterization of an RNA/DNA binding motif in the N-terminal domain of RecQ4 helicases.,Marino F, Mojumdar A, Zucchelli C, Bhardwaj A, Buratti E, Vindigni A, Musco G, Onesti S Sci Rep. 2016 Feb 18;6:21501. doi: 10.1038/srep21501. PMID:26888063[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Marino F, Mojumdar A, Zucchelli C, Bhardwaj A, Buratti E, Vindigni A, Musco G, Onesti S. Structural and biochemical characterization of an RNA/DNA binding motif in the N-terminal domain of RecQ4 helicases. Sci Rep. 2016 Feb 18;6:21501. doi: 10.1038/srep21501. PMID:26888063 doi:http://dx.doi.org/10.1038/srep21501
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