5okc: Difference between revisions

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==Crystal structure of the Ctf18-1-8 module from Ctf18-RFC==
==Crystal structure of the Ctf18-1-8 module from Ctf18-RFC==
<StructureSection load='5okc' size='340' side='right' caption='[[5okc]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='5okc' size='340' side='right'caption='[[5okc]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5okc]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OKC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OKC FirstGlance]. <br>
<table><tr><td colspan='2'>[[5okc]] is a 6 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=5OKC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OKC FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></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]] 2.3&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></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=5okc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5okc OCA], [http://pdbe.org/5okc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5okc RCSB], [http://www.ebi.ac.uk/pdbsum/5okc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5okc ProSAT]</span></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=5okc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5okc OCA], [https://pdbe.org/5okc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5okc RCSB], [https://www.ebi.ac.uk/pdbsum/5okc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5okc ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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>  [[http://www.uniprot.org/uniprot/CTF18_YEAST CTF18_YEAST]] Essential for the fidelity of chromosome transmission. Required for the DNA replication block checkpoint. 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:11287619</ref> <ref>PMID:11389843</ref> <ref>PMID:11486023</ref> <ref>PMID:15964801</ref>  [[http://www.uniprot.org/uniprot/CTF8_YEAST CTF8_YEAST]] Essential for the fidelity of chromosome transmission. Required for the DNA replication block checkpoint. 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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Grabarczyk, D B]]
[[Category: Large Structures]]
[[Category: Kisker, C]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Clamp loader dna-binding protein triple beta-barrel domain winged-helix domain]]
[[Category: Grabarczyk DB]]
[[Category: Replication]]
[[Category: Kisker C]]

Latest revision as of 19:52, 13 December 2023

Crystal structure of the Ctf18-1-8 module from Ctf18-RFCCrystal structure of the Ctf18-1-8 module from Ctf18-RFC

Structural highlights

5okc is a 6 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 2.3Å
Ligands:, ,
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

Ctf18-RFC is an alternative PCNA loader which plays important but poorly understood roles in multiple DNA replication-associated processes. To fulfill its specialist roles, the Ctf18-RFC clamp loader contains a unique module in which the Dcc1-Ctf8 complex is bound to the C terminus of Ctf18 (the Ctf18-1-8 module). Here, we report the structural and functional characterization of the heterotetrameric complex formed between Ctf18-1-8 and a 63 kDa fragment of DNA polymerase varepsilon. Our data reveal that Ctf18-1-8 binds stably to the polymerase and far from its other functional sites, suggesting that Ctf18-RFC could be associated with Pol varepsilon throughout normal replication as the leading strand clamp loader. We also show that Pol varepsilon and double-stranded DNA compete to bind the same winged-helix domain on Dcc1, with Pol varepsilon being the preferred binding partner, thus suggesting that there are two alternative pathways to recruit Ctf18-RFC to sites of replication.

Structural Basis for the Recruitment of Ctf18-RFC to the Replisome.,Grabarczyk DB, Silkenat S, Kisker C Structure. 2017 Dec 6. pii: S0969-2126(17)30357-X. doi:, 10.1016/j.str.2017.11.004. PMID:29225079[3]

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

References

  1. 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
  2. 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
  3. Grabarczyk DB, Silkenat S, Kisker C. Structural Basis for the Recruitment of Ctf18-RFC to the Replisome. Structure. 2017 Dec 6. pii: S0969-2126(17)30357-X. doi:, 10.1016/j.str.2017.11.004. PMID:29225079 doi:http://dx.doi.org/10.1016/j.str.2017.11.004

5okc, resolution 2.30Å

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