5oun
From Proteopedia
(Difference between revisions)
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<StructureSection load='5oun' size='340' side='right' caption='[[5oun]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='5oun' size='340' side='right' caption='[[5oun]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5oun]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OUN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OUN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5oun]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OUN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OUN 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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RVB2, TIH2, TIP49B, YPL235W, P1060 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=5oun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oun OCA], [http://pdbe.org/5oun PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oun RCSB], [http://www.ebi.ac.uk/pdbsum/5oun PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oun 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=5oun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oun OCA], [http://pdbe.org/5oun PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oun RCSB], [http://www.ebi.ac.uk/pdbsum/5oun PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oun ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/RUVB2_YEAST RUVB2_YEAST]] DNA helicase which participates in several chromatin remodeling complexes, including the SWR1 and the INO80 complexes. The SWR1 complex mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. The INO80 complex remodels chromatin by shifting nucleosomes. Its ability to induce transcription of some phosphate-responsive genes is modulated by inositol polyphosphates. The INO80 complex is involved in DNA repair by associating to 'Ser-129' phosphorylated H2A histones as a response to DNA damage. During transcription may recruit SPT15/TBP to the TATA-boxes of involved genes. Required for box C/D and box H/ACA snoRNA accumulation and involved in pre-rRNA processing.<ref>PMID:10787406</ref> <ref>PMID:10952318</ref> <ref>PMID:11278922</ref> <ref>PMID:11604509</ref> <ref>PMID:12576485</ref> <ref>PMID:14645854</ref> <ref>PMID:14690608</ref> <ref>PMID:15045029</ref> <ref>PMID:15525518</ref> | [[http://www.uniprot.org/uniprot/RUVB2_YEAST RUVB2_YEAST]] DNA helicase which participates in several chromatin remodeling complexes, including the SWR1 and the INO80 complexes. The SWR1 complex mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. The INO80 complex remodels chromatin by shifting nucleosomes. Its ability to induce transcription of some phosphate-responsive genes is modulated by inositol polyphosphates. The INO80 complex is involved in DNA repair by associating to 'Ser-129' phosphorylated H2A histones as a response to DNA damage. During transcription may recruit SPT15/TBP to the TATA-boxes of involved genes. Required for box C/D and box H/ACA snoRNA accumulation and involved in pre-rRNA processing.<ref>PMID:10787406</ref> <ref>PMID:10952318</ref> <ref>PMID:11278922</ref> <ref>PMID:11604509</ref> <ref>PMID:12576485</ref> <ref>PMID:14645854</ref> <ref>PMID:14690608</ref> <ref>PMID:15045029</ref> <ref>PMID:15525518</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | We report the nearly complete (1)H, (15)N and (13)C resonance assignment and the solution structure of the external DII domain of the yeast Rvb2 protein, a member of the AAA+ATPase superfamily. | ||
| + | |||
| + | NMR assignment and solution structure of the external DII domain of the yeast Rvb2 protein.,Bragantini B, Rouillon C, Charpentier B, Manival X, Quinternet M Biomol NMR Assign. 2018 Mar 22. pii: 10.1007/s12104-018-9816-5. doi:, 10.1007/s12104-018-9816-5. PMID:29569106<ref>PMID:29569106</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5oun" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Atcc 18824]] | ||
[[Category: DNA helicase]] | [[Category: DNA helicase]] | ||
[[Category: Bragantini, B]] | [[Category: Bragantini, B]] | ||
Revision as of 06:50, 4 April 2018
NMR solution structure of the external DII domain of Rvb2 from Saccharomyces cerevisiae
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