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6tng

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'''Unreleased structure'''
 
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The entry 6tng is ON HOLD until Dec 07 2021
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==Structure of FANCD2 in complex with FANCI==
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<SX load='6tng' size='340' side='right' viewer='molstar' caption='[[6tng]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6tng]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TNG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TNG 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">Electron Microscopy, [[Resolution|Resolution]] 4.1&#8491;</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=6tng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tng OCA], [https://pdbe.org/6tng PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tng RCSB], [https://www.ebi.ac.uk/pdbsum/6tng PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tng ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/F1NP22_CHICK F1NP22_CHICK]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Vertebrate DNA crosslink repair excises toxic replication-blocking DNA crosslinks. Numerous factors involved in crosslink repair have been identified, and mutations in their corresponding genes cause Fanconi anemia (FA). A key step in crosslink repair is monoubiquitination of the FANCD2-FANCI heterodimer, which then recruits nucleases to remove the DNA lesion. Here, we use cryo-EM to determine the structures of recombinant chicken FANCD2 and FANCI complexes. FANCD2-FANCI adopts a closed conformation when the FANCD2 subunit is monoubiquitinated, creating a channel that encloses double-stranded DNA (dsDNA). Ubiquitin is positioned at the interface of FANCD2 and FANCI, where it acts as a covalent molecular pin to trap the complex on DNA. In contrast, isolated FANCD2 is a homodimer that is unable to bind DNA, suggestive of an autoinhibitory mechanism that prevents premature activation. Together, our work suggests that FANCD2-FANCI is a clamp that is locked onto DNA by ubiquitin, with distinct interfaces that may recruit other DNA repair factors.
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Authors:
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FANCD2-FANCI is a clamp stabilized on DNA by monoubiquitination of FANCD2 during DNA repair.,Alcon P, Shakeel S, Chen ZA, Rappsilber J, Patel KJ, Passmore LA Nat Struct Mol Biol. 2020 Feb 17. pii: 10.1038/s41594-020-0380-1. doi:, 10.1038/s41594-020-0380-1. PMID:32066963<ref>PMID:32066963</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 6tng" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</SX>
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[[Category: Gallus gallus]]
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[[Category: Large Structures]]
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[[Category: Alcon P]]
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[[Category: Passmore LA]]
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[[Category: Shakeel S]]

Current revision

Structure of FANCD2 in complex with FANCI

6tng, resolution 4.10Å

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