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| | ==Structure of human RECQ-like helicase in complex with an oligonucleotide== | | ==Structure of human RECQ-like helicase in complex with an oligonucleotide== |
| - | <StructureSection load='4u7d' size='340' side='right' caption='[[4u7d]], [[Resolution|resolution]] 3.40Å' scene=''> | + | <StructureSection load='4u7d' size='340' side='right'caption='[[4u7d]], [[Resolution|resolution]] 3.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4u7d]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U7D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4U7D FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4u7d]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=4U7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4U7D 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='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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RECQL, RECQ1, RECQL1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4u7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u7d OCA], [https://pdbe.org/4u7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4u7d RCSB], [https://www.ebi.ac.uk/pdbsum/4u7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4u7d ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </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=4u7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u7d OCA], [http://pdbe.org/4u7d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4u7d RCSB], [http://www.ebi.ac.uk/pdbsum/4u7d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4u7d ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RECQ1_HUMAN RECQ1_HUMAN]] DNA helicase that may play a role in the repair of DNA that is damaged by ultraviolet light or other mutagens. Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction.<ref>PMID:15886194</ref> <ref>PMID:7961977</ref> <ref>PMID:8056767</ref> | + | [https://www.uniprot.org/uniprot/RECQ1_HUMAN RECQ1_HUMAN] DNA helicase that may play a role in the repair of DNA that is damaged by ultraviolet light or other mutagens. Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction.<ref>PMID:15886194</ref> <ref>PMID:7961977</ref> <ref>PMID:8056767</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4u7d" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4u7d" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Helicase 3D structures|Helicase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: DNA helicase]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]] | + | [[Category: Large Structures]] |
| - | [[Category: Arrowsmith, C H]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Bountra, C]] | + | [[Category: Arrowsmith CH]] |
| - | [[Category: Cooper, C D.O]] | + | [[Category: Bountra C]] |
| - | [[Category: Delft, F von]] | + | [[Category: Cooper CDO]] |
| - | [[Category: Edwards, A]] | + | [[Category: Edwards A]] |
| - | [[Category: Gileadi, O]] | + | [[Category: Gileadi O]] |
| - | [[Category: Pike, A C.W]] | + | [[Category: Pike ACW]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Schnecke C]] |
| - | [[Category: Schnecke, C]] | + | [[Category: Zhang Y]] |
| - | [[Category: Zhang, Y]] | + | [[Category: Von Delft F]] |
| - | [[Category: Dna binding protein]] | + | |
| - | [[Category: Dna strand annealing]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Hydrolase-dna complex]]
| + | |
| - | [[Category: Nuclear protein]]
| + | |
| - | [[Category: Sgc]]
| + | |
| Structural highlights
Function
RECQ1_HUMAN DNA helicase that may play a role in the repair of DNA that is damaged by ultraviolet light or other mutagens. Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction.[1] [2] [3]
Publication Abstract from PubMed
RecQ helicases are a widely conserved family of ATP-dependent motors with diverse roles in nearly every aspect of bacterial and eukaryotic genome maintenance. However, the physical mechanisms by which RecQ helicases recognize and process specific DNA replication and repair intermediates are largely unknown. Here, we solved crystal structures of the human RECQ1 helicase in complexes with tailed-duplex DNA and ssDNA. The structures map the interactions of the ssDNA tail and the branch point along the helicase and Zn-binding domains, which, together with reported structures of other helicases, define the catalytic stages of helicase action. We also identify a strand-separating pin, which (uniquely in RECQ1) is buttressed by the protein dimer interface. A duplex DNA-binding surface on the C-terminal domain is shown to play a role in DNA unwinding, strand annealing, and Holliday junction (HJ) branch migration. We have combined EM and analytical ultracentrifugation approaches to show that RECQ1 can form what appears to be a flat, homotetrameric complex and propose that RECQ1 tetramers are involved in HJ recognition. This tetrameric arrangement suggests a platform for coordinated activity at the advancing and receding duplexes of an HJ during branch migration.
Human RECQ1 helicase-driven DNA unwinding, annealing, and branch migration: Insights from DNA complex structures.,Pike AC, Gomathinayagam S, Swuec P, Berti M, Zhang Y, Schnecke C, Marino F, von Delft F, Renault L, Costa A, Gileadi O, Vindigni A Proc Natl Acad Sci U S A. 2015 Apr 7;112(14):4286-91. doi:, 10.1073/pnas.1417594112. Epub 2015 Mar 23. PMID:25831490[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Doherty KM, Sharma S, Uzdilla LA, Wilson TM, Cui S, Vindigni A, Brosh RM Jr. RECQ1 helicase interacts with human mismatch repair factors that regulate genetic recombination. J Biol Chem. 2005 Jul 29;280(30):28085-94. Epub 2005 May 9. PMID:15886194 doi:http://dx.doi.org/10.1074/jbc.M500265200
- ↑ Puranam KL, Blackshear PJ. Cloning and characterization of RECQL, a potential human homologue of the Escherichia coli DNA helicase RecQ. J Biol Chem. 1994 Nov 25;269(47):29838-45. PMID:7961977
- ↑ Seki M, Yanagisawa J, Kohda T, Sonoyama T, Ui M, Enomoto T. Purification of two DNA-dependent adenosinetriphosphatases having DNA helicase activity from HeLa cells and comparison of the properties of the two enzymes. J Biochem. 1994 Mar;115(3):523-31. PMID:8056767
- ↑ Pike AC, Gomathinayagam S, Swuec P, Berti M, Zhang Y, Schnecke C, Marino F, von Delft F, Renault L, Costa A, Gileadi O, Vindigni A. Human RECQ1 helicase-driven DNA unwinding, annealing, and branch migration: Insights from DNA complex structures. Proc Natl Acad Sci U S A. 2015 Apr 7;112(14):4286-91. doi:, 10.1073/pnas.1417594112. Epub 2015 Mar 23. PMID:25831490 doi:http://dx.doi.org/10.1073/pnas.1417594112
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