6j0x

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<StructureSection load='6j0x' size='340' side='right'caption='[[6j0x]], [[Resolution|resolution]] 2.31&Aring;' scene=''>
<StructureSection load='6j0x' size='340' side='right'caption='[[6j0x]], [[Resolution|resolution]] 2.31&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6j0x]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J0X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6J0X FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6j0x]] is a 8 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=6J0X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6J0X FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6j0w|6j0w]]</td></tr>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6j0w|6j0w]]</td></tr>
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<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]), MMS22, SLM2, YLR320W ([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=6j0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j0x OCA], [http://pdbe.org/6j0x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6j0x RCSB], [http://www.ebi.ac.uk/pdbsum/6j0x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6j0x 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=6j0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j0x OCA], [http://pdbe.org/6j0x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6j0x RCSB], [http://www.ebi.ac.uk/pdbsum/6j0x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6j0x 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/MMS22_YEAST MMS22_YEAST]] Substrate targeting component of a cullin-RING-based E3 ubiquitin-protein ligase complex RTT101(MMS1-MMS22). RTT101(MMS1-MMS22) promotes fork progression through damaged DNA or natural pause sites by stabilizing replication proteins like the replication fork-pausing complex (FPC) and leading-strand polymerase at stalled replication forks. RTT101(MMS1-MMS22) ubiquitinates the acetylated histones H3K56ac-H4 at lysine residues H3K121, H3K122 and H3K125. Ubiquitination is required for efficient histone deposition during replication-coupled nucleosome assembly, probably by facilitating the transfer of H3-H4 from ASF1 to other chaperones involved in histone deposition.<ref>PMID:12482937</ref> <ref>PMID:12694535</ref> <ref>PMID:15718301</ref> <ref>PMID:16024805</ref> <ref>PMID:18321796</ref> <ref>PMID:18704118</ref> <ref>PMID:21593207</ref> <ref>PMID:24209620</ref>
[[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/MMS22_YEAST MMS22_YEAST]] Substrate targeting component of a cullin-RING-based E3 ubiquitin-protein ligase complex RTT101(MMS1-MMS22). RTT101(MMS1-MMS22) promotes fork progression through damaged DNA or natural pause sites by stabilizing replication proteins like the replication fork-pausing complex (FPC) and leading-strand polymerase at stalled replication forks. RTT101(MMS1-MMS22) ubiquitinates the acetylated histones H3K56ac-H4 at lysine residues H3K121, H3K122 and H3K125. Ubiquitination is required for efficient histone deposition during replication-coupled nucleosome assembly, probably by facilitating the transfer of H3-H4 from ASF1 to other chaperones involved in histone deposition.<ref>PMID:12482937</ref> <ref>PMID:12694535</ref> <ref>PMID:15718301</ref> <ref>PMID:16024805</ref> <ref>PMID:18321796</ref> <ref>PMID:18704118</ref> <ref>PMID:21593207</ref> <ref>PMID:24209620</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6j0x" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[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 Mms22

PDB ID 6j0x

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