6j0w
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='6j0w' size='340' side='right'caption='[[6j0w]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='6j0w' size='340' side='right'caption='[[6j0w]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6j0w]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J0W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6J0W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6j0w]] 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=6J0W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6J0W FirstGlance]. <br> |
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6j0v|6j0v]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6j0v|6j0v]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RTT107, ESC4, YHR154W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), KRE29, YER038C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=6j0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j0w OCA], [http://pdbe.org/6j0w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6j0w RCSB], [http://www.ebi.ac.uk/pdbsum/6j0w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6j0w 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=6j0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j0w OCA], [http://pdbe.org/6j0w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6j0w RCSB], [http://www.ebi.ac.uk/pdbsum/6j0w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6j0w ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/RT107_YEAST RT107_YEAST]] Required for resumption of chromosome replication after DNA damage, specifically in S phase. Is recruited to chromatin in the presence of RTT109 and RTT101 in response to stalled replication forks and acts as a scaffold during DNA repair.<ref>PMID:14988729</ref> <ref>PMID:17978089</ref> [[http://www.uniprot.org/uniprot/KRE29_YEAST KRE29_YEAST]] Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks. | [[http://www.uniprot.org/uniprot/RT107_YEAST RT107_YEAST]] Required for resumption of chromosome replication after DNA damage, specifically in S phase. Is recruited to chromatin in the presence of RTT109 and RTT101 in response to stalled replication forks and acts as a scaffold during DNA repair.<ref>PMID:14988729</ref> <ref>PMID:17978089</ref> [[http://www.uniprot.org/uniprot/KRE29_YEAST KRE29_YEAST]] Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | BRCT domains support myriad protein-protein interactions involved in genome maintenance. Although di-BRCT recognition of phospho-proteins is well known to support the genotoxic response, whether multi-BRCT domains can acquire distinct structures and functions is unclear. Here we present the tetra-BRCT structures from the conserved yeast protein Rtt107 in free and ligand-bound forms. The four BRCT repeats fold into a tetrahedral structure that recognizes unmodified ligands using a bi-partite mechanism, suggesting repeat origami enabling function acquisition. Functional studies show that Rtt107 binding of partner proteins of diverse activities promotes genome replication and stability in both distinct and concerted manners. A unified theme is that tetra- and di-BRCT domains of Rtt107 collaborate to recruit partner proteins to chromatin. Our work thus illustrates how a master regulator uses two types of BRCT domains to recognize distinct genome factors and direct them to chromatin for constitutive genome protection. | ||
| + | |||
| + | Molecular Basis for Control of Diverse Genome Stability Factors by the Multi-BRCT Scaffold Rtt107.,Wan B, Wu J, Meng X, Lei M, Zhao X Mol Cell. 2019 Jul 25;75(2):238-251.e5. doi: 10.1016/j.molcel.2019.05.035. Epub, 2019 Jul 16. PMID:31348879<ref>PMID:31348879</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6j0w" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Baker's yeast]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Lei, M]] | [[Category: Lei, M]] | ||
Revision as of 10:19, 26 February 2020
Crystal Structure of Yeast Rtt107 and Nse6
| |||||||||||
