4ccg: Difference between revisions

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<StructureSection load='4ccg' size='340' side='right'caption='[[4ccg]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='4ccg' size='340' side='right'caption='[[4ccg]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4ccg]] is a 4 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=4CCG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CCG FirstGlance]. <br>
<table><tr><td colspan='2'>[[4ccg]] is a 4 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=4CCG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CCG FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<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=4ccg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ccg OCA], [http://pdbe.org/4ccg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ccg RCSB], [http://www.ebi.ac.uk/pdbsum/4ccg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ccg ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ccg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ccg OCA], [https://pdbe.org/4ccg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ccg RCSB], [https://www.ebi.ac.uk/pdbsum/4ccg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ccg ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
[[http://www.uniprot.org/uniprot/FANCL_HUMAN FANCL_HUMAN]] Fanconi anemia. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/UBE2T_HUMAN UBE2T_HUMAN]] Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes monoubiquitination. Involved in mitomycin-C (MMC)-induced DNA repair: acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway. Also mediates monoubiquitination of FANCL and FANCI. May contribute to ubiquitination and degradation of BRCA1. In vitro able to promote polyubiquitination using all 7 ubiquitin Lys residues, but may prefer 'Lys-11'-, 'Lys-27'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination.<ref>PMID:16916645</ref> <ref>PMID:17938197</ref> <ref>PMID:19111657</ref> <ref>PMID:19887602</ref> <ref>PMID:19589784</ref> <ref>PMID:20061386</ref>  [[http://www.uniprot.org/uniprot/FANCL_HUMAN FANCL_HUMAN]] Ubiquitin ligase protein that mediates monoubiquitination of FANCD2, a key step in the DNA damage pathway. Also mediates monoubiquitination of FANCI. May stimulate the ubiquitin release from UBE2W. May be required for proper primordial germ cell proliferation in the embryonic stage, whereas it is probably not needed for spermatogonial proliferation after birth.<ref>PMID:12973351</ref> <ref>PMID:16916645</ref> <ref>PMID:17938197</ref> <ref>PMID:19111657</ref> <ref>PMID:19589784</ref> 
[[https://www.uniprot.org/uniprot/UBE2T_HUMAN UBE2T_HUMAN]] Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes monoubiquitination. Involved in mitomycin-C (MMC)-induced DNA repair: acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway. Also mediates monoubiquitination of FANCL and FANCI. May contribute to ubiquitination and degradation of BRCA1. In vitro able to promote polyubiquitination using all 7 ubiquitin Lys residues, but may prefer 'Lys-11'-, 'Lys-27'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination.<ref>PMID:16916645</ref> <ref>PMID:17938197</ref> <ref>PMID:19111657</ref> <ref>PMID:19887602</ref> <ref>PMID:19589784</ref> <ref>PMID:20061386</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The combination of an E2 ubiquitin-conjugating enzyme with an E3 ubiquitin-ligase is essential for ubiquitin modification of a substrate. Moreover, the pairing dictates both the substrate choice and the modification type. The molecular details of generic E3-E2 interactions are well established. Nevertheless, the determinants of selective, specific E3-E2 recognition are not understood. There are approximately 40 E2s and approximately 600 E3s giving rise to a possible approximately 24,000 E3-E2 pairs. Using the Fanconi Anemia pathway exclusive E3-E2 pair, FANCL-Ube2T, we report the atomic structure of the FANCL RING-Ube2T complex, revealing a specific and extensive network of additional electrostatic and hydrophobic interactions. Furthermore, we show that these specific interactions are required for selection of Ube2T over other E2s by FANCL.
 
Structure of the Human FANCL RING-Ube2T Complex Reveals Determinants of Cognate E3-E2 Selection.,Hodson C, Purkiss A, Miles JA, Walden H Structure. 2013 Dec 31. pii: S0969-2126(13)00466-8. doi:, 10.1016/j.str.2013.12.004. PMID:24389026<ref>PMID:24389026</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ccg" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Ubiquitin conjugating enzyme|Ubiquitin conjugating enzyme]]
*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
*[[Ubiquitin protein ligase|Ubiquitin protein ligase]]
*[[3D structures of ubiquitin conjugating enzyme|3D structures of ubiquitin conjugating enzyme]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Hodson, C]]
[[Category: Hodson C]]
[[Category: Purkiss, A]]
[[Category: Purkiss A]]
[[Category: Walden, H]]
[[Category: Walden H]]
[[Category: Ligase]]
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