5okc: Difference between revisions
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<StructureSection load='5okc' size='340' side='right' caption='[[5okc]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='5okc' size='340' side='right' caption='[[5okc]], [[Resolution|resolution]] 2.30Å' 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 [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=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> | ||
</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='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> | ||
<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='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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DCC1, YCL016C, YCL16C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), CTF8, YHR191C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), CTF18, CHL12, YMR078C, YM9582.03C ([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=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'>[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> | ||
</table> | </table> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Baker's yeast]] | |||
[[Category: Grabarczyk, D B]] | [[Category: Grabarczyk, D B]] | ||
[[Category: Kisker, C]] | [[Category: Kisker, C]] | ||
[[Category: Clamp loader dna-binding protein triple beta-barrel domain winged-helix domain]] | [[Category: Clamp loader dna-binding protein triple beta-barrel domain winged-helix domain]] | ||
[[Category: Replication]] | [[Category: Replication]] | ||
Revision as of 11:39, 10 January 2018
Crystal structure of the Ctf18-1-8 module from Ctf18-RFCCrystal structure of the Ctf18-1-8 module from Ctf18-RFC
Structural highlights
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] [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.[3] [4] [5] [6] [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.[7] [8] Publication Abstract from PubMedCtf18-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[9] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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