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| | ==Crystal structure of the C-terminal part of Fun30 ATPase domain== | | ==Crystal structure of the C-terminal part of Fun30 ATPase domain== |
| - | <StructureSection load='5gn1' size='340' side='right' caption='[[5gn1]], [[Resolution|resolution]] 1.95Å' scene=''> | + | <StructureSection load='5gn1' size='340' side='right'caption='[[5gn1]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5gn1]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GN1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GN1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5gn1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GN1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GN1 FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</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=5gn1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gn1 OCA], [http://pdbe.org/5gn1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gn1 RCSB], [http://www.ebi.ac.uk/pdbsum/5gn1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gn1 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=5gn1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gn1 OCA], [https://pdbe.org/5gn1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gn1 RCSB], [https://www.ebi.ac.uk/pdbsum/5gn1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gn1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FUN30_YEAST FUN30_YEAST]] DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is both required for DNA repair and heterochromatin organization. Promotes DNA end resection of double-strand breaks (DSBs) following DNA damage: probably acts by weakening histone DNA interactions in nucleosomes flanking DSBs, facilitating single-stranded DNA (ssDNA) production by the EXO1 and SGS1 machinery. Promotes gene silencing at heterochromatin by regulating the chromatin structure within or around silent loci. Also required for heterochromatin organization at centromeres.<ref>PMID:19956593</ref> <ref>PMID:20075079</ref> <ref>PMID:22960743</ref> <ref>PMID:22960744</ref> <ref>PMID:23007155</ref> <ref>PMID:23028372</ref> | + | [https://www.uniprot.org/uniprot/FUN30_YEAST FUN30_YEAST] DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is both required for DNA repair and heterochromatin organization. Promotes DNA end resection of double-strand breaks (DSBs) following DNA damage: probably acts by weakening histone DNA interactions in nucleosomes flanking DSBs, facilitating single-stranded DNA (ssDNA) production by the EXO1 and SGS1 machinery. Promotes gene silencing at heterochromatin by regulating the chromatin structure within or around silent loci. Also required for heterochromatin organization at centromeres.<ref>PMID:19956593</ref> <ref>PMID:20075079</ref> <ref>PMID:22960743</ref> <ref>PMID:22960744</ref> <ref>PMID:23007155</ref> <ref>PMID:23028372</ref> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | Fun30 (Function unknown now 30) is a chromatin remodeller belonging to the Snf2 family. It has previously been reported to be a regulator of several cellular activities, including DNA repair, gene silencing and maintenance of chromatin structure. Here, the crystal structure of the Fun30 ATPase-C domain (the C-lobe of the ATPase domain) is reported at 1.95 A resolution. Although the structure displays overall similarities to those of other Snf2 family members, a new structural module was found to be specific to the Fun30 subfamily. Fun30 ATPase-C was shown be monomeric in solution and showed no detectable affinity for dsDNA. |
| | + | |
| | + | Crystal structure of the ATPase-C domain of the chromatin remodeller Fun30 from Saccharomyces cerevisiae.,Liu L, Jiang T Acta Crystallogr F Struct Biol Commun. 2017 Jan 1;73(Pt 1):9-15. doi:, 10.1107/S2053230X16019269. Epub 2017 Jan 1. PMID:28045388<ref>PMID:28045388</ref> |
| | + | |
| | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | + | </div> |
| | + | <div class="pdbe-citations 5gn1" 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: Large Structures]] |
| - | [[Category: Jiang, T]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Liu, L]] | + | [[Category: Jiang T]] |
| - | [[Category: Helicase]] | + | [[Category: Liu L]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Reca]]
| + | |
| - | [[Category: Remodeler]]
| + | |
| Structural highlights
Function
FUN30_YEAST DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is both required for DNA repair and heterochromatin organization. Promotes DNA end resection of double-strand breaks (DSBs) following DNA damage: probably acts by weakening histone DNA interactions in nucleosomes flanking DSBs, facilitating single-stranded DNA (ssDNA) production by the EXO1 and SGS1 machinery. Promotes gene silencing at heterochromatin by regulating the chromatin structure within or around silent loci. Also required for heterochromatin organization at centromeres.[1] [2] [3] [4] [5] [6]
Publication Abstract from PubMed
Fun30 (Function unknown now 30) is a chromatin remodeller belonging to the Snf2 family. It has previously been reported to be a regulator of several cellular activities, including DNA repair, gene silencing and maintenance of chromatin structure. Here, the crystal structure of the Fun30 ATPase-C domain (the C-lobe of the ATPase domain) is reported at 1.95 A resolution. Although the structure displays overall similarities to those of other Snf2 family members, a new structural module was found to be specific to the Fun30 subfamily. Fun30 ATPase-C was shown be monomeric in solution and showed no detectable affinity for dsDNA.
Crystal structure of the ATPase-C domain of the chromatin remodeller Fun30 from Saccharomyces cerevisiae.,Liu L, Jiang T Acta Crystallogr F Struct Biol Commun. 2017 Jan 1;73(Pt 1):9-15. doi:, 10.1107/S2053230X16019269. Epub 2017 Jan 1. PMID:28045388[7]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Neves-Costa A, Will WR, Vetter AT, Miller JR, Varga-Weisz P. The SNF2-family member Fun30 promotes gene silencing in heterochromatic loci. PLoS One. 2009 Dec 1;4(12):e8111. doi: 10.1371/journal.pone.0008111. PMID:19956593 doi:http://dx.doi.org/10.1371/journal.pone.0008111
- ↑ Awad S, Ryan D, Prochasson P, Owen-Hughes T, Hassan AH. The Snf2-homolog Fun30 acts as a homodimeric ATP-dependent chromatin-remodeling enzyme. J Biol Chem. 2010 Jan 14. PMID:20075079 doi:http://dx.doi.org/M109.082149
- ↑ Chen X, Cui D, Papusha A, Zhang X, Chu CD, Tang J, Chen K, Pan X, Ira G. The Fun30 nucleosome remodeller promotes resection of DNA double-strand break ends. Nature. 2012 Sep 27;489(7417):576-80. doi: 10.1038/nature11355. Epub 2012 Sep 9. PMID:22960743 doi:http://dx.doi.org/10.1038/nature11355
- ↑ Costelloe T, Louge R, Tomimatsu N, Mukherjee B, Martini E, Khadaroo B, Dubois K, Wiegant WW, Thierry A, Burma S, van Attikum H, Llorente B. The yeast Fun30 and human SMARCAD1 chromatin remodellers promote DNA end resection. Nature. 2012 Sep 27;489(7417):581-4. doi: 10.1038/nature11353. Epub 2012 Sep 9. PMID:22960744 doi:http://dx.doi.org/10.1038/nature11353
- ↑ Eapen VV, Sugawara N, Tsabar M, Wu WH, Haber JE. The Saccharomyces cerevisiae chromatin remodeler Fun30 regulates DNA end resection and checkpoint deactivation. Mol Cell Biol. 2012 Nov;32(22):4727-40. doi: 10.1128/MCB.00566-12. Epub 2012 Sep , 24. PMID:23007155 doi:http://dx.doi.org/10.1128/MCB.00566-12
- ↑ Durand-Dubief M, Will WR, Petrini E, Theodorou D, Harris RR, Crawford MR, Paszkiewicz K, Krueger F, Correra RM, Vetter AT, Miller JR, Kent NA, Varga-Weisz P. SWI/SNF-like chromatin remodeling factor Fun30 supports point centromere function in S. cerevisiae. PLoS Genet. 2012 Sep;8(9):e1002974. doi: 10.1371/journal.pgen.1002974. Epub 2012 , Sep 27. PMID:23028372 doi:http://dx.doi.org/10.1371/journal.pgen.1002974
- ↑ Liu L, Jiang T. Crystal structure of the ATPase-C domain of the chromatin remodeller Fun30 from Saccharomyces cerevisiae. Acta Crystallogr F Struct Biol Commun. 2017 Jan 1;73(Pt 1):9-15. doi:, 10.1107/S2053230X16019269. Epub 2017 Jan 1. PMID:28045388 doi:http://dx.doi.org/10.1107/S2053230X16019269
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