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3l82

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{{STRUCTURE_3l82| PDB=3l82 | SCENE= }}
 
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===X-ray Crystal structure of TRF1 and Fbx4 complex===
 
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{{ABSTRACT_PUBMED_20159592}}
 
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==Function==
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==X-ray Crystal structure of TRF1 and Fbx4 complex==
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<StructureSection load='3l82' size='340' side='right' caption='[[3l82]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3l82]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L82 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3L82 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=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TERF1, PIN2, TRBF1, TRF, TRF1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), FBXO4, FBX4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3l82 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l82 OCA], [http://pdbe.org/3l82 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3l82 RCSB], [http://www.ebi.ac.uk/pdbsum/3l82 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3l82 ProSAT]</span></td></tr>
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</table>
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== Function ==
[[http://www.uniprot.org/uniprot/TERF1_HUMAN TERF1_HUMAN]] Binds the telomeric double-stranded TTAGGG repeat and negatively regulates telomere length. Involved in the regulation of the mitotic spindle. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways.<ref>PMID:16166375</ref> [[http://www.uniprot.org/uniprot/FBX4_HUMAN FBX4_HUMAN]] Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes ubiquitination of CCND1 and its subsequent proteasomal degradation. Recognizes TERF1 and promotes its ubiquitination together with UBE2D1.<ref>PMID:10531035</ref> <ref>PMID:16275645</ref> <ref>PMID:18598945</ref> <ref>PMID:20159592</ref> <ref>PMID:20181953</ref>
[[http://www.uniprot.org/uniprot/TERF1_HUMAN TERF1_HUMAN]] Binds the telomeric double-stranded TTAGGG repeat and negatively regulates telomere length. Involved in the regulation of the mitotic spindle. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways.<ref>PMID:16166375</ref> [[http://www.uniprot.org/uniprot/FBX4_HUMAN FBX4_HUMAN]] Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes ubiquitination of CCND1 and its subsequent proteasomal degradation. Recognizes TERF1 and promotes its ubiquitination together with UBE2D1.<ref>PMID:10531035</ref> <ref>PMID:16275645</ref> <ref>PMID:18598945</ref> <ref>PMID:20159592</ref> <ref>PMID:20181953</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l8/3l82_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=3l82 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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TRF1 is a critical regulator of telomere length. As such, TRF1 levels are regulated by ubiquitin-dependent proteolysis via an SCF E3 ligase where Fbx4 contributes to substrate specification. Here, we report the crystal structure of the Fbx4-TRF1 complex at 2.4 A resolution. Fbx4 contains an unusual substrate-binding domain that adopts a small GTPase fold. Strikingly, this atypical GTPase domain of Fbx4 binds to a globular domain of TRF1 through an intermolecular beta sheet, instead of recognizing short peptides/degrons as often seen in other F-box protein-substrate complexes. Importantly, mutations in this interface abrogate Fbx4-dependent TRF1 binding and ubiquitination. Furthermore, the data demonstrate that recognition of TRF1 by SCF(Fbx4) is regulated by another telomere protein, TIN2. Our results reveal an atypical small GTPase domain within Fbx4 as a substrate-binding motif for SCF(Fbx4) and uncover a mechanism for selective ubiquitination and degradation of TRF1 in telomere homeostasis control.
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==About this Structure==
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Structural basis of selective ubiquitination of TRF1 by SCFFbx4.,Zeng Z, Wang W, Yang Y, Chen Y, Yang X, Diehl JA, Liu X, Lei M Dev Cell. 2010 Feb 16;18(2):214-25. PMID:20159592<ref>PMID:20159592</ref>
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[[3l82]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L82 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:020159592</ref><references group="xtra"/><references/>
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</div>
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[[Category: Homo sapiens]]
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<div class="pdbe-citations 3l82" style="background-color:#fffaf0;"></div>
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[[Category: Chen, Y.]]
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== References ==
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[[Category: Diehl, J A.]]
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<references/>
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[[Category: Lei, M.]]
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__TOC__
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[[Category: Liu, X D.]]
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</StructureSection>
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[[Category: Wang, W.]]
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[[Category: Human]]
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[[Category: Yang, X M.]]
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[[Category: Chen, Y]]
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[[Category: Yang, Y T.]]
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[[Category: Diehl, J A]]
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[[Category: Zeng, Z X.]]
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[[Category: Lei, M]]
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[[Category: Liu, X D]]
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[[Category: Wang, W]]
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[[Category: Yang, X M]]
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[[Category: Yang, Y T]]
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[[Category: Zeng, Z X]]
[[Category: Adp-ribosylation]]
[[Category: Adp-ribosylation]]
[[Category: Cell cycle]]
[[Category: Cell cycle]]

Current revision

X-ray Crystal structure of TRF1 and Fbx4 complex

3l82, resolution 2.40Å

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