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5msn

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Structure of the Dcc1 Protein

Structural highlights

5msn is a 4 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.002Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DCC1_YEAST Component of the RFC-like complex CTF18-RFC which is required for efficient establishment of chromosome cohesion during S-phase and may load or unload POL30/PCNA. During a clamp loading circle, the RFC:clamp complex binds to DNA and the recognition of the double-stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The complex presumably provides bipartite ATP sites in which one subunit supplies a catalytic site for hydrolysis of ATP bound to the neighboring subunit. Dissociation of RFC from the clamp leaves the clamp encircling DNA.^[1] ^[2]

Publication Abstract from PubMed

Replication factor C complexes load and unload processivity clamps from DNA and are involved in multiple DNA replication and repair pathways. The RFCCtf18 variant complex is required for activation of the intra-S-phase checkpoint at stalled replication forks and aids the establishment of sister chromatid cohesion. Unlike other RFC complexes, RFCCtf18 contains two non-Rfc subunits, Dcc1 and Ctf8. Here, we present the crystal structure of the Dcc1-Ctf8 heterodimer bound to the C-terminus of Ctf18. We find that the C-terminus of Dcc1 contains three-winged helix domains, which bind to both ssDNA and dsDNA We further show that these domains are required for full recruitment of the complex to chromatin, and correct activation of the replication checkpoint. These findings provide the first structural data on a eukaryotic seven-subunit clamp loader and define a new biochemical activity for Dcc1.

Structural studies of RFCCtf18 reveal a novel chromatin recruitment role for Dcc1.,Wade BO, Liu HW, Samora CP, Uhlmann F, Singleton MR EMBO Rep. 2017 Feb 10. pii: e201642825. doi: 10.15252/embr.201642825. PMID:28188145^[3]

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

References

↑ Mayer ML, Gygi SP, Aebersold R, Hieter P. Identification of RFC(Ctf18p, Ctf8p, Dcc1p): an alternative RFC complex required for sister chromatid cohesion in S. cerevisiae. Mol Cell. 2001 May;7(5):959-70. PMID:11389843
↑ Bylund GO, Burgers PM. Replication protein A-directed unloading of PCNA by the Ctf18 cohesion establishment complex. Mol Cell Biol. 2005 Jul;25(13):5445-55. PMID:15964801 doi:http://dx.doi.org/25/13/5445
↑ Wade BO, Liu HW, Samora CP, Uhlmann F, Singleton MR. Structural studies of RFCCtf18 reveal a novel chromatin recruitment role for Dcc1. EMBO Rep. 2017 Feb 10. pii: e201642825. doi: 10.15252/embr.201642825. PMID:28188145 doi:http://dx.doi.org/10.15252/embr.201642825

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/5msn"

Categories: Large Structures | Saccharomyces cerevisiae S288C | Singleton MR | Wade BO

@@ Line 3: / Line 3: @@
 <StructureSection load='5msn' size='340' side='right'caption='[[5msn]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5msn]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MSN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5MSN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5msn]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MSN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MSN FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5msn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5msn OCA], [http://pdbe.org/5msn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5msn RCSB], [http://www.ebi.ac.uk/pdbsum/5msn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5msn ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.002&#8491;</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=5msn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5msn OCA], [https://pdbe.org/5msn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5msn RCSB], [https://www.ebi.ac.uk/pdbsum/5msn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5msn ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/DCC1_YEAST DCC1_YEAST]] Component of the RFC-like complex CTF18-RFC which is required for efficient establishment of chromosome cohesion during S-phase and may load or unload POL30/PCNA. During a clamp loading circle, the RFC:clamp complex binds to DNA and the recognition of the double-stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The complex presumably provides bipartite ATP sites in which one subunit supplies a catalytic site for hydrolysis of ATP bound to the neighboring subunit. Dissociation of RFC from the clamp leaves the clamp encircling DNA.<ref>PMID:11389843</ref> <ref>PMID:15964801</ref>
+[https://www.uniprot.org/uniprot/DCC1_YEAST DCC1_YEAST] Component of the RFC-like complex CTF18-RFC which is required for efficient establishment of chromosome cohesion during S-phase and may load or unload POL30/PCNA. During a clamp loading circle, the RFC:clamp complex binds to DNA and the recognition of the double-stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The complex presumably provides bipartite ATP sites in which one subunit supplies a catalytic site for hydrolysis of ATP bound to the neighboring subunit. Dissociation of RFC from the clamp leaves the clamp encircling DNA.<ref>PMID:11389843</ref> <ref>PMID:15964801</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 23: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Singleton, M R]]
+[[Category: Saccharomyces cerevisiae S288C]]
-[[Category: Wade, B O]]
+[[Category: Singleton MR]]
-[[Category: Cell cycle]]
+[[Category: Wade BO]]
-[[Category: Dna repair]]
-[[Category: Winged-helix]]

5msn

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Current revision

Structure of the Dcc1 Protein

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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