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| - | ==Crystal structure of Rad4-Rad23 crosslinked to a normal DNA duplex==
| + | #REDIRECT [[4yir]] This PDB entry is obsolete and replaced by 4yir |
| - | <StructureSection load='4u29' size='340' side='right' caption='[[4u29]], [[Resolution|resolution]] 3.05Å' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[4u29]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U29 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4U29 FirstGlance]. <br>
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| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=G47:N2-ETHANETHIOL-2-DEOXY-GUANOSINE-5-MONOPHOSPHATE'>G47</scene></td></tr>
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| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2qsf|2qsf]], [[2qsg|2qsg]], [[2qsh|2qsh]]</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=4u29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u29 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4u29 RCSB], [http://www.ebi.ac.uk/pdbsum/4u29 PDBsum]</span></td></tr>
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| - | </table>
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| - | == Function ==
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| - | [[http://www.uniprot.org/uniprot/RAD4_YEAST RAD4_YEAST]] Involved in nucleotide excision repair of DNA damaged with UV light, bulky adducts, or cross-linking agents. [[http://www.uniprot.org/uniprot/RAD23_YEAST RAD23_YEAST]] Plays a central role both in proteasomal degradation of misfolded proteins and DNA repair. Central component of a complex required to couple deglycosylation and proteasome-mediated degradation of misfolded proteins in the endoplasmic reticulum that are retrotranslocated in the cytosol. Involved in DNA excision repair. May play a part in DNA damage recognition and/or in altering chromatin structure to allow access by damage-processing enzymes.
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| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | The xeroderma pigmentosum C (XPC) complex initiates nucleotide excision repair by recognizing DNA lesions before recruiting downstream factors. How XPC detects structurally diverse lesions embedded within normal DNA is unknown. Here we present a crystal structure that captures the yeast XPC orthologue (Rad4) on a single register of undamaged DNA. The structure shows that a disulphide-tethered Rad4 flips out normal nucleotides and adopts a conformation similar to that seen with damaged DNA. Contrary to many DNA repair enzymes that can directly reject non-target sites as structural misfits, our results suggest that Rad4/XPC uses a kinetic gating mechanism whereby lesion selectivity arises from the kinetic competition between DNA opening and the residence time of Rad4/XPC per site. This mechanism is further supported by measurements of Rad4-induced lesion-opening times using temperature-jump perturbation spectroscopy. Kinetic gating may be a general mechanism used by site-specific DNA-binding proteins to minimize time-consuming interrogations of non-target sites.
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| - | Kinetic gating mechanism of DNA damage recognition by Rad4/XPC.,Chen X, Velmurugu Y, Zheng G, Park B, Shim Y, Kim Y, Liu L, Van Houten B, He C, Ansari A, Min JH Nat Commun. 2015 Jan 6;6:5849. doi: 10.1038/ncomms6849. PMID:25562780<ref>PMID:25562780</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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| - | == References ==
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| - | <references/>
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| - | __TOC__
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| - | </StructureSection>
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| - | [[Category: Chen, X]]
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| - | [[Category: Kim, Y]]
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| - | [[Category: Min, J H]]
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| - | [[Category: Beta-hairpin]]
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| - | [[Category: Disulfide crosslinking]]
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| - | [[Category: Dna binding protein-dna complex]]
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| - | [[Category: Dna damage repair]]
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| - | [[Category: Nucleotide excision repair]]
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| - | [[Category: Protein-dna complex]]
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| - | [[Category: Protein-dna crosslinking]]
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| - | [[Category: Protein-dna interaction]]
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| - | [[Category: Transglutaminase domain]]
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| - | [[Category: Xeroderma pigmentosum]]
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