5hh7

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==crystal structure of Arabidopsis ORC1b BAH-PHD cassette in complex with unmodified H3 peptide==
==crystal structure of Arabidopsis ORC1b BAH-PHD cassette in complex with unmodified H3 peptide==
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<StructureSection load='5hh7' size='340' side='right' caption='[[5hh7]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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<StructureSection load='5hh7' size='340' side='right'caption='[[5hh7]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5hh7]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HH7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HH7 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5hh7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HH7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HH7 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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">X-ray diffraction, [[Resolution|Resolution]] 1.901&#8491;</td></tr>
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<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=5hh7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hh7 OCA], [http://pdbe.org/5hh7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hh7 RCSB], [http://www.ebi.ac.uk/pdbsum/5hh7 PDBsum]</span></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=ZN:ZINC+ION'>ZN</scene></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=5hh7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hh7 OCA], [https://pdbe.org/5hh7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hh7 RCSB], [https://www.ebi.ac.uk/pdbsum/5hh7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hh7 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ORC1B_ARATH ORC1B_ARATH]] Essential protein required for ovules fertilization (PubMed:15634699, PubMed:19171893). 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 (By similarity). H3K4me3 effector that regulates positively the transcription of a subset of genes (PubMed:19171893).[UniProtKB:P54784]<ref>PMID:15634699</ref> <ref>PMID:19171893</ref>
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[https://www.uniprot.org/uniprot/ORC1B_ARATH ORC1B_ARATH] Essential protein required for ovules fertilization (PubMed:15634699, PubMed:19171893). 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 (By similarity). H3K4me3 effector that regulates positively the transcription of a subset of genes (PubMed:19171893).[UniProtKB:P54784]<ref>PMID:15634699</ref> <ref>PMID:19171893</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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DNA replication initiation relies on the formation of the origin recognition complex (ORC). The plant ORC subunit 1 (ORC1) protein possesses a conserved N-terminal BAH domain with an embedded plant-specific PHD finger, whose function may be potentially regulated by an epigenetic mechanism. Here, we report structural and biochemical studies on the Arabidopsis thaliana ORC1b BAH-PHD cassette which specifically recognizes the unmodified H3 tail. The crystal structure of ORC1b BAH-PHD cassette in complex with an H3(1-15) peptide reveals a strict requirement for the unmodified state of R2, T3, and K4 on the H3 tail and a novel multivalent BAH and PHD readout mode for H3 peptide recognition. Such recognition may contribute to epigenetic regulation of the initiation of DNA replication.
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Structural Basis for the Unique Multivalent Readout of Unmodified H3 Tail by Arabidopsis ORC1b BAH-PHD Cassette.,Li S, Yang Z, Du X, Liu R, Wilkinson AW, Gozani O, Jacobsen SE, Patel DJ, Du J Structure. 2016 Mar 1;24(3):486-94. doi: 10.1016/j.str.2016.01.004. Epub 2016 Feb, 11. PMID:26876097<ref>PMID:26876097</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5hh7" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Du, J]]
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[[Category: Arabidopsis thaliana]]
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[[Category: Li, S]]
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[[Category: Large Structures]]
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[[Category: Bah domain]]
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[[Category: Du J]]
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[[Category: Multivalent readout]]
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[[Category: Li S]]
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[[Category: Phd finger]]
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[[Category: Transcription]]
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Current revision

crystal structure of Arabidopsis ORC1b BAH-PHD cassette in complex with unmodified H3 peptide

PDB ID 5hh7

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