5dgo

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'''Unreleased structure'''
 
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The entry 5dgo is ON HOLD
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==Crystal structure of cell division cycle protein 45 (Cdc45)==
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<StructureSection load='5dgo' size='340' side='right'caption='[[5dgo]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5dgo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DGO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DGO FirstGlance]. <br>
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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]] 2.1&#8491;</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5dgo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dgo OCA], [https://pdbe.org/5dgo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dgo RCSB], [https://www.ebi.ac.uk/pdbsum/5dgo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dgo ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CDC45_HUMAN CDC45_HUMAN] Required for initiation of chromosomal DNA replication.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Cell division cycle protein 45 (Cdc45) is required for DNA synthesis during genome duplication, as a component of the Cdc45-MCM-GINS (CMG) helicase. Despite its essential biological function, its biochemical role in DNA replication has remained elusive. Here we report the 2.1-A crystal structure of human Cdc45, which confirms its evolutionary link with the bacterial RecJ nuclease and reveals several unexpected features that underpin its function in eukaryotic DNA replication. These include a long-range interaction between N- and C-terminal DHH domains, blocking access to the DNA-binding groove of its RecJ-like fold, and a helical insertion in its N-terminal DHH domain, which appears poised for replisome interactions. In combination with available electron microscopy data, we validate by mutational analysis the mechanism of Cdc45 association with the MCM ring and GINS co-activator, critical for CMG assembly. These findings provide an indispensable molecular basis to rationalize the essential role of Cdc45 in genomic duplication.
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Authors:
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Structure of human Cdc45 and implications for CMG helicase function.,Simon AC, Sannino V, Costanzo V, Pellegrini L Nat Commun. 2016 May 18;7:11638. doi: 10.1038/ncomms11638. PMID:27189187<ref>PMID:27189187</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5dgo" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Pellegrini L]]
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[[Category: Simon AC]]

Current revision

Crystal structure of cell division cycle protein 45 (Cdc45)

PDB ID 5dgo

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