3l40
From Proteopedia
(Difference between revisions)
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==Crystal Structure of S. pombe Brc1 BRCT5-BRCT6 domains== | ==Crystal Structure of S. pombe Brc1 BRCT5-BRCT6 domains== | ||
- | <StructureSection load='3l40' size='340' side='right' caption='[[3l40]], [[Resolution|resolution]] 1.55Å' scene=''> | + | <StructureSection load='3l40' size='340' side='right'caption='[[3l40]], [[Resolution|resolution]] 1.55Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3l40]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3l40]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L40 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L40 FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55Å</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=3l40 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l40 OCA], [https://pdbe.org/3l40 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l40 RCSB], [https://www.ebi.ac.uk/pdbsum/3l40 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l40 ProSAT]</span></td></tr> | |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [https://www.uniprot.org/uniprot/BRC1_SCHPO BRC1_SCHPO] Required for mitotic fidelity, specifically in the G2 phase of the cell cycle. Plays a role in chromatin organization. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3l40 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3l40 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | ATM(Tel1) and ATR(Rad3) checkpoint kinases phosphorylate the C-terminus of histone H2AX (H2A in yeasts) in chromatin flanking DNA damage, establishing a recruitment platform for checkpoint and repair proteins. Phospho-H2A/X (gammaH2A/X)-binding proteins at double-strand breaks (DSBs) have been characterized, but those required for replication stress responses are unknown. Here, we present genetic, biochemical, small angle X-ray scattering (SAXS), and X-ray structural studies of the Schizosaccharomyces pombe Brc1, a 6-BRCT-domain protein that is structurally related to Saccharomyces cerevisiae Rtt107 and mammalian PTIP. Brc1 binds gammaH2A to form spontaneous and DNA damage-induced nuclear foci. Spontaneous Brc1 foci colocalize with ribosomal DNA repeats, a region prone to fork pausing and genomic instability, whereas DNA damage-induced Brc1 foci colocalize with DSB response factors. gammaH2A binding is critical for Brc1 function. The 1.45 A resolution crystal structure of Brc1-gammaH2A complex shows how variable BRCT insertion loops sculpt tandem-BRCT phosphoprotein-binding pockets to facilitate unique phosphoprotein-interaction specificities, and unveils an acidic DNA-mimicking Brc1 surface. From these results, Brc1 docking to gammaH2A emerges as a critical chromatin-specific response to replication-associated DNA damage. | ||
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- | gammaH2A binds Brc1 to maintain genome integrity during S-phase.,Williams JS, Williams RS, Dovey CL, Guenther G, Tainer JA, Russell P EMBO J. 2010 Mar 17;29(6):1136-48. Epub 2010 Jan 21. PMID:20094029<ref>PMID:20094029</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 3l40" style="background-color:#fffaf0;"></div> | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: | + | [[Category: Schizosaccharomyces pombe]] |
- | [[Category: | + | [[Category: Guenther G]] |
- | [[Category: | + | [[Category: Tainer JA]] |
- | [[Category: Williams | + | [[Category: Williams JS]] |
- | [[Category: | + | [[Category: Williams RS]] |
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Current revision
Crystal Structure of S. pombe Brc1 BRCT5-BRCT6 domains
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