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| <SX load='5zr1' size='340' side='right' viewer='molstar' caption='[[5zr1]], [[Resolution|resolution]] 3.00Å' scene=''> | | <SX load='5zr1' size='340' side='right' viewer='molstar' caption='[[5zr1]], [[Resolution|resolution]] 3.00Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[5zr1]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZR1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ZR1 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[5zr1]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [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=5ZR1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZR1 FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3Å</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=5zr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zr1 OCA], [http://pdbe.org/5zr1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zr1 RCSB], [http://www.ebi.ac.uk/pdbsum/5zr1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zr1 ProSAT]</span></td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=5zr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zr1 OCA], [https://pdbe.org/5zr1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zr1 RCSB], [https://www.ebi.ac.uk/pdbsum/5zr1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zr1 ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/ORC6_YEAST ORC6_YEAST]] Component of the origin recognition complex (ORC) that binds origins of replication. It has a role in both chromosomal replication and mating type transcriptional silencing. Binds to the ARS consensus sequence (ACS) of origins of replication.<ref>PMID:17825064</ref> <ref>PMID:18006685</ref> [[http://www.uniprot.org/uniprot/ORC3_YEAST ORC3_YEAST]] Component of the origin recognition complex (ORC) that binds origins of replication. It has a role in both chromosomal replication and mating type transcriptional silencing. Binds to the ARS consensus sequence (ACS) of origins of replication.<ref>PMID:18006685</ref> [[http://www.uniprot.org/uniprot/ORC2_YEAST ORC2_YEAST]] Component of the origin recognition complex (ORC) that binds origins of replication. It has a role in both chromosomal replication and mating type transcriptional silencing. Binds to the ARS consensus sequence (ACS) of origins of replication.<ref>PMID:17825064</ref> [[http://www.uniprot.org/uniprot/ORC1_YEAST ORC1_YEAST]] Component of the origin recognition complex (ORC) that binds origins of replication. It has a role in both chromosomal replication and mating type transcriptional silencing. Binds to the ARS consensus sequence (ACS) of origins of replication.<ref>PMID:17825064</ref> [[http://www.uniprot.org/uniprot/ORC4_YEAST ORC4_YEAST]] Component of the origin recognition complex (ORC) that binds origins of replication. It has a role in both chromosomal replication and mating type transcriptional silencing. Binds to the ARS consensus sequence (ACS) of origins of replication. [[http://www.uniprot.org/uniprot/ORC5_YEAST ORC5_YEAST]] Component of the origin recognition complex (ORC) that binds origins of replication. It has a role in both chromosomal replication and mating type transcriptional silencing. Binds to the ARS consensus sequence (ACS) of origins of replication. This subunit is a candidate for the mediation of ATP-dependent binding of ORC to origins. May also be a substrate targeting component of a cullin-RING-based E3 ubiquitin-protein ligase complex RTT101(MMS1-ORC5).<ref>PMID:18006685</ref> | | [https://www.uniprot.org/uniprot/ORC2_YEAST ORC2_YEAST] Component of the origin recognition complex (ORC) that binds origins of replication. It has a role in both chromosomal replication and mating type transcriptional silencing. Binds to the ARS consensus sequence (ACS) of origins of replication.<ref>PMID:17825064</ref> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| The six-subunit origin recognition complex (ORC) binds to DNA to mark the site for the initiation of replication in eukaryotes. Here we report a 3 A cryo-electron microscopy structure of the Saccharomyces cerevisiae ORC bound to a 72-base-pair origin DNA sequence that contains the ARS consensus sequence (ACS) and the B1 element. The ORC encircles DNA through extensive interactions with both phosphate backbone and bases, and bends DNA at the ACS and B1 sites. Specific recognition of thymine residues in the ACS is carried out by a conserved basic amino acid motif of Orc1 in the minor groove, and by a species-specific helical insertion motif of Orc4 in the major groove. Moreover, similar insertions into major and minor grooves are also embedded in the B1 site by basic patch motifs from Orc2 and Orc5, respectively, to contact bases and to bend DNA. This work pinpoints a conserved role of ORC in modulating DNA structure to facilitate origin selection and helicase loading in eukaryotes.
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| Structure of the origin recognition complex bound to DNA replication origin.,Li N, Lam WH, Zhai Y, Cheng J, Cheng E, Zhao Y, Gao N, Tye BK Nature. 2018 Jul;559(7713):217-222. doi: 10.1038/s41586-018-0293-x. Epub 2018 Jul, 4. PMID:29973722<ref>PMID:29973722</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 5zr1" style="background-color:#fffaf0;"></div>
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| == References == | | == References == |
| <references/> | | <references/> |
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| </SX> | | </SX> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Cheng, E]] | | [[Category: Saccharomyces cerevisiae]] |
| [[Category: Cheng, J]] | | [[Category: Saccharomyces cerevisiae S288C]] |
| [[Category: Gao, N]] | | [[Category: Cheng E]] |
| [[Category: Lam, W H]] | | [[Category: Cheng J]] |
| [[Category: Li, N]] | | [[Category: Gao N]] |
| [[Category: Tye, B K]] | | [[Category: Lam WH]] |
| [[Category: Zhai, Y]] | | [[Category: Li N]] |
| [[Category: Zhao, Y]] | | [[Category: Tye BK]] |
| [[Category: 72-bp origin dna]] | | [[Category: Zhai Y]] |
| [[Category: Dna binding protein]] | | [[Category: Zhao Y]] |
| [[Category: Dna binding protein-dna complex]]
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| [[Category: Dna replication initiation]]
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| [[Category: Origin recognition complex]]
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