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| <StructureSection load='1zhi' size='340' side='right'caption='[[1zhi]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='1zhi' size='340' side='right'caption='[[1zhi]], [[Resolution|resolution]] 2.70Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[1zhi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZHI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZHI FirstGlance]. <br> | | <table><tr><td colspan='2'>[[1zhi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZHI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZHI FirstGlance]. <br> |
| </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1z1a|1z1a]], [[1m4z|1m4z]]</div></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]] 2.7Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ORC1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), SIR1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=1zhi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zhi OCA], [https://pdbe.org/1zhi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zhi RCSB], [https://www.ebi.ac.uk/pdbsum/1zhi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zhi 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=1zhi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zhi OCA], [https://pdbe.org/1zhi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zhi RCSB], [https://www.ebi.ac.uk/pdbsum/1zhi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zhi ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[https://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> [[https://www.uniprot.org/uniprot/SIR1_YEAST SIR1_YEAST]] Involved in the establishment, but not the maintenance, of heterochromatic silencing at the cryptic mating-type loci HMR and HML. Is recruited by interacting with the ORC1 subunit of the origin recognition complex (ORC), which binds to HML-I or HMR-E silencers, DNA elements that direct the formation of silent chromatin at the mating-type loci. Establishes transcriptional silencing by recruiting the three other SIR proteins, SIR2, SIR3, and SIR4, that function directly in silenced chromatin and establish repression. Also found in centromeric chromatin. Binds to and helps retain CAC1, a subunit of chromatin assembly factor I (CAF-I) at centromeric loci independent on the other SIR proteins.<ref>PMID:8221892</ref> <ref>PMID:8622770</ref> <ref>PMID:12134062</ref>
| | [https://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> |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zhi ConSurf]. | | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zhi ConSurf]. |
| <div style="clear:both"></div> | | <div style="clear:both"></div> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| The Sir1 protein plays a key role in establishing a silent chromatin structure at the cryptic mating-type loci HMR and HML in Saccharomyces cerevisiae by interacting with the bromo-adjacent homology (BAH) domain of the Orc1p subunit of the origin recognition complex (ORC). Here, we present the high-resolution crystal structures of the ORC interaction region (OIR) of Sir1p and that of the complex formed between the OIR and BAH domains. Amino acids within the OIR previously shown to be required for a Sir1p/ORC interaction are presented on a conserved, convex surface that forms a complementary interface with a concave region of the Orc1 BAH domain that is critical for transcriptional silencing. The OIR/BAH interaction surface comprises a network of hydrophobic and polar/ionic interactions between discrete structural modules in each protein and involves several residues that were not implicated in previous studies. These data provide important structural insights into a protein-protein interaction critical for the formation of a specialized chromatin domain within eukaryotic chromosomes.
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| Structural basis of the Sir1-origin recognition complex interaction in transcriptional silencing.,Hou Z, Bernstein DA, Fox CA, Keck JL Proc Natl Acad Sci U S A. 2005 Jun 14;102(24):8489-94. Epub 2005 Jun 2. PMID:15932939<ref>PMID:15932939</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 1zhi" style="background-color:#fffaf0;"></div>
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| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Atcc 18824]]
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Bernstein, D A]] | | [[Category: Saccharomyces cerevisiae]] |
| [[Category: Fox, C A]] | | [[Category: Bernstein DA]] |
| [[Category: Hou, Z]] | | [[Category: Fox CA]] |
| [[Category: Keck, J L]] | | [[Category: Hou Z]] |
| [[Category: Bah domain]] | | [[Category: Keck JL]] |
| [[Category: Oir domain]]
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| [[Category: Protein complex]]
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| [[Category: Transcription-replication complex]]
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