5gn1

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Current revision (11:36, 2 August 2023) (edit) (undo)
 
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<StructureSection load='5gn1' size='340' side='right'caption='[[5gn1]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
<StructureSection load='5gn1' size='340' side='right'caption='[[5gn1]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5gn1]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. 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>
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<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>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FUN30 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
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<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>
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<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>
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<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>
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</table>
</table>
== Function ==
== Function ==
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[[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>
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[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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Baker's yeast]]
 
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[[Category: DNA helicase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Jiang, T]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Liu, L]]
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[[Category: Jiang T]]
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[[Category: Helicase]]
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[[Category: Liu L]]
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[[Category: Hydrolase]]
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[[Category: Reca]]
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[[Category: Remodeler]]
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Current revision

Crystal structure of the C-terminal part of Fun30 ATPase domain

PDB ID 5gn1

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