8ir2

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of the SLF1 BRCT domain in complex with a Rad18 peptide containing pS442 and pS444

Structural highlights

8ir2 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.75Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SLF1_HUMAN Plays a role in the DNA damage response (DDR) pathway by regulating postreplication repair of UV-damaged DNA and genomic stability maintenance (PubMed:25931565). The SLF1-SLF2 complex acts to link RAD18 with the SMC5-SMC6 complex at replication-coupled interstrand cross-links (ICL) and DNA double-strand breaks (DSBs) sites on chromatin during DNA repair in response to stalled replication forks (PubMed:25931565). Promotes the recruitment of SLF2 and the SMC5-SMC6 complex to DNA lesions (PubMed:25931565, PubMed:36373674).^[1] ^[2]

Publication Abstract from PubMed

Rad18 interacts with the SMC5/6 localization factor 1 (SLF1) to recruit the SMC5/6 complex to DNA damage sites for repair. The mechanism of the specific Rad18 recognition by SLF1 is unclear. Here, we present the crystal structure of the tandem BRCT repeat (tBRCT) in SLF1 (SLF1(tBRCT)) bound with the interacting Rad18 peptide. Our structure and biochemical studies demonstrate that SLF1(tBRCT) interacts with two phosphoserines and adjacent residues in Rad18 for high-affinity and specificity Rad18 recognition. We found that SLF1(tBRCT) utilizes mechanisms common among tBRCTs as well as unique ones for Rad18 binding, the latter include interactions with an alpha-helical structure in Rad18 that has not been observed in other tBRCT-bound ligand proteins. Our work provides structural insights into Rad18 targeting by SLF1 and expands the understanding of BRCT-mediated complex assembly.

Structural insights into Rad18 targeting by the SLF1 BRCT domains.,Huang W, Qiu F, Zheng L, Shi M, Shen M, Zhao X, Xiang S J Biol Chem. 2023 Nov;299(11):105288. doi: 10.1016/j.jbc.2023.105288. Epub 2023 , Sep 23. PMID:37748650^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Räschle M, Smeenk G, Hansen RK, Temu T, Oka Y, Hein MY, Nagaraj N, Long DT, Walter JC, Hofmann K, Storchova Z, Cox J, Bekker-Jensen S, Mailand N, Mann M. DNA repair. Proteomics reveals dynamic assembly of repair complexes during bypass of DNA cross-links. Science. 2015 May 1;348(6234):1253671. PMID:25931565 doi:10.1126/science.1253671
↑ Oravcova M, Nie M, Zilio N, Maeda S, Jami-Alahmadi Y, Lazzerini-Denchi E, Wohlschlegel JA, Ulrich HD, Otomo T, Boddy MN. The Nse5/6-like SIMC1-SLF2 complex localizes SMC5/6 to viral replication centers. Elife. 2022 Nov 14;11:e79676. doi: 10.7554/eLife.79676. PMID:36373674 doi:http://dx.doi.org/10.7554/eLife.79676
↑ Huang W, Qiu F, Zheng L, Shi M, Shen M, Zhao X, Xiang S. Structural insights into Rad18 targeting by the SLF1 BRCT domains. J Biol Chem. 2023 Sep 23;299(11):105288. PMID:37748650 doi:10.1016/j.jbc.2023.105288

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/8ir2"

Categories: Homo sapiens | Large Structures | Huang W | Qiu F | Xiang S

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 8ir2 is ON HOLD  until Paper Publication
+==Crystal structure of the SLF1 BRCT domain in complex with a Rad18 peptide containing pS442 and pS444==
+<StructureSection load='8ir2' size='340' side='right'caption='[[8ir2]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8ir2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8IR2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IR2 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></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=8ir2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ir2 OCA], [https://pdbe.org/8ir2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ir2 RCSB], [https://www.ebi.ac.uk/pdbsum/8ir2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ir2 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/SLF1_HUMAN SLF1_HUMAN] Plays a role in the DNA damage response (DDR) pathway by regulating postreplication repair of UV-damaged DNA and genomic stability maintenance (PubMed:25931565). The SLF1-SLF2 complex acts to link RAD18 with the SMC5-SMC6 complex at replication-coupled interstrand cross-links (ICL) and DNA double-strand breaks (DSBs) sites on chromatin during DNA repair in response to stalled replication forks (PubMed:25931565). Promotes the recruitment of SLF2 and the SMC5-SMC6 complex to DNA lesions (PubMed:25931565, PubMed:36373674).<ref>PMID:25931565</ref> <ref>PMID:36373674</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Rad18 interacts with the SMC5/6 localization factor 1 (SLF1) to recruit the SMC5/6 complex to DNA damage sites for repair. The mechanism of the specific Rad18 recognition by SLF1 is unclear. Here, we present the crystal structure of the tandem BRCT repeat (tBRCT) in SLF1 (SLF1(tBRCT)) bound with the interacting Rad18 peptide. Our structure and biochemical studies demonstrate that SLF1(tBRCT) interacts with two phosphoserines and adjacent residues in Rad18 for high-affinity and specificity Rad18 recognition. We found that SLF1(tBRCT) utilizes mechanisms common among tBRCTs as well as unique ones for Rad18 binding, the latter include interactions with an alpha-helical structure in Rad18 that has not been observed in other tBRCT-bound ligand proteins. Our work provides structural insights into Rad18 targeting by SLF1 and expands the understanding of BRCT-mediated complex assembly.
-Authors:
+Structural insights into Rad18 targeting by the SLF1 BRCT domains.,Huang W, Qiu F, Zheng L, Shi M, Shen M, Zhao X, Xiang S J Biol Chem. 2023 Nov;299(11):105288. doi: 10.1016/j.jbc.2023.105288. Epub 2023 , Sep 23. PMID:37748650<ref>PMID:37748650</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 8ir2" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Huang W]]
+[[Category: Qiu F]]
+[[Category: Xiang S]]

8ir2

From Proteopedia

Current revision

Crystal structure of the SLF1 BRCT domain in complex with a Rad18 peptide containing pS442 and pS444

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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