6skl

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<StructureSection load='6skl' size='340' side='right'caption='[[6skl]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
<StructureSection load='6skl' size='340' side='right'caption='[[6skl]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6skl]] is a 18 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=6SKL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6SKL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6skl]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SKL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SKL FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.7&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MCM2, YBL023C, YBL0438 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), SLD5, YDR489W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), CDC45, SLD4, YLR103C, L8004.11 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), CTF4, CHL15, POB1, YPR135W, P9659.7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), TOF1, YNL273W, N0636 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), CSM3, YMR048W, YM9796.01 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), MCM3, YEL032W, SYGP-ORF23 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), MCM4, CDC54, HCD21, YPR019W, YP9531.13 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), MCM5, CDC46, YLR274W, L9328.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), MCM6, YGL201C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), MCM7, CDC47, YBR202W, YBR1441 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), PSF1, YDR013W, PZA208, YD8119.18 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), PSF2, YJL072C, HRF213, J1086 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), PSF3, YOL146W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6skl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6skl OCA], [https://pdbe.org/6skl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6skl RCSB], [https://www.ebi.ac.uk/pdbsum/6skl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6skl ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6skl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6skl OCA], [http://pdbe.org/6skl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6skl RCSB], [http://www.ebi.ac.uk/pdbsum/6skl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6skl ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CDC45_YEAST CDC45_YEAST]] Required for initiation of chromosomal DNA replication. Acts at the origin of replication. Also has a role in minichromosome maintenance.<ref>PMID:8901577</ref> <ref>PMID:9001208</ref> [[http://www.uniprot.org/uniprot/PSF1_YEAST PSF1_YEAST]] Required for DNA replication. Functions as part of the GINS complex which plays an essential role in the initiation of DNA replication by binding to DNA replication origins and facilitating the assembly of the DNA replication machinery. Required for the chromatin binding of CDC45.<ref>PMID:12730134</ref> [[http://www.uniprot.org/uniprot/MCM3_YEAST MCM3_YEAST]] Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity. Necessary for cell growth.<ref>PMID:19896182</ref> <ref>PMID:19910535</ref> [[http://www.uniprot.org/uniprot/MCM2_YEAST MCM2_YEAST]] Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity; specifically the MCM2-MCM5 association is proposed to be reversible and to mediate a open ring conformation which may facilitate DNA loading. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity. Necessary for cell growth.<ref>PMID:19896182</ref> <ref>PMID:19910535</ref> [[http://www.uniprot.org/uniprot/CSM3_YEAST CSM3_YEAST]] Forms a fork protection complex (FPC) with TOF1 which is required for chromosome segregation during meiosis and DNA damage repair. FPC coordinates leading and lagging strand synthesis and moves with the replication fork. FPC stabilizes replication forks in a configuration that is recognized by replication checkpoint sensors and protects stalled replication forks against the fork-releasing activity of RRM3 helicase.<ref>PMID:11470404</ref> <ref>PMID:14742714</ref> <ref>PMID:15282308</ref> <ref>PMID:15755447</ref> <ref>PMID:16024805</ref> <ref>PMID:16219777</ref> <ref>PMID:16418273</ref> [[http://www.uniprot.org/uniprot/MCM7_YEAST MCM7_YEAST]] Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity.<ref>PMID:19896182</ref> <ref>PMID:19910535</ref> [[http://www.uniprot.org/uniprot/MCM4_YEAST MCM4_YEAST]] Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity. Required for S phase execution.<ref>PMID:19896182</ref> <ref>PMID:19910535</ref> [[http://www.uniprot.org/uniprot/PSF3_YEAST PSF3_YEAST]] Functions as part of the GINS complex which plays an essential role in the initiation of DNA replication by binding to DNA replication origins and facilitating the assembly of the DNA replication machinery.[UniProtKB:P40359]<ref>PMID:12730134</ref> [[http://www.uniprot.org/uniprot/CTF4_YEAST CTF4_YEAST]] Accessory factor for DNA replication. It plays a role in accurately duplicating the genome in vivo. [[http://www.uniprot.org/uniprot/TOF1_YEAST TOF1_YEAST]] Forms a fork protection complex (FPC) with CSM3 and which is required for chromosome segregation during meiosis and DNA damage repair. FPC coordinates leading and lagging strand synthesis and moves with the replication fork. FPC stabilizes replication forks in a configuration that is recognized by replication checkpoint sensors and protects stalled replication forks against the fork-releasing activity of RRM3 helicase.<ref>PMID:11156979</ref> <ref>PMID:12944972</ref> <ref>PMID:14742714</ref> <ref>PMID:15598824</ref> <ref>PMID:15755447</ref> <ref>PMID:16024805</ref> <ref>PMID:16137625</ref> <ref>PMID:16219777</ref> <ref>PMID:16418273</ref> [[http://www.uniprot.org/uniprot/PSF2_YEAST PSF2_YEAST]] Functions as part of the GINS complex which plays an essential role in the initiation of DNA replication by binding to DNA replication origins and facilitating the assembly of the DNA replication machinery.<ref>PMID:12730134</ref> [[http://www.uniprot.org/uniprot/MCM5_YEAST MCM5_YEAST]] Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity; specifically the MCM2-MCM5 association is proposed to be reversible and to mediate a open ring conformation which may facilitate DNA loading. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity.<ref>PMID:19896182</ref> <ref>PMID:19910535</ref> [[http://www.uniprot.org/uniprot/SLD5_YEAST SLD5_YEAST]] Required for DNA replication. Functions as part of the GINS complex which plays an essential role in the initiation of DNA replication by binding to DNA replication origins and facilitating the assembly of the DNA replication machinery.<ref>PMID:12730134</ref> [UniProtKB:P40359] [[http://www.uniprot.org/uniprot/MCM6_YEAST MCM6_YEAST]] Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity. Required for the entry in S phase and for cell division.<ref>PMID:19896182</ref> <ref>PMID:19910535</ref>
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[https://www.uniprot.org/uniprot/PSF1_YEAST PSF1_YEAST] Required for DNA replication. Functions as part of the GINS complex which plays an essential role in the initiation of DNA replication by binding to DNA replication origins and facilitating the assembly of the DNA replication machinery. Required for the chromatin binding of CDC45.<ref>PMID:12730134</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Baker's yeast]]
 
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[[Category: DNA helicase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Baretic, D]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Jenkyn-Bedford, M]]
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[[Category: Synthetic construct]]
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[[Category: Yeeles, J]]
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[[Category: Baretic D]]
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[[Category: Aaa+ helicase]]
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[[Category: Jenkyn-Bedford M]]
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[[Category: Cip-box]]
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[[Category: Yeeles J]]
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[[Category: Cmg]]
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[[Category: Fork dna]]
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[[Category: Fork protection complex]]
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[[Category: Gin]]
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[[Category: Mcm]]
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[[Category: Protein-dna complex]]
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[[Category: Replication]]
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[[Category: Replisome]]
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Current revision

Cryo-EM structure of the CMG Fork Protection Complex at a replication fork - Conformation 1

PDB ID 6skl

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