5wy5

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==Crystal structure of MAGEG1 and NSE1 complex==
==Crystal structure of MAGEG1 and NSE1 complex==
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<StructureSection load='5wy5' size='340' side='right' caption='[[5wy5]], [[Resolution|resolution]] 2.92&Aring;' scene=''>
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<StructureSection load='5wy5' size='340' side='right'caption='[[5wy5]], [[Resolution|resolution]] 2.92&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5wy5]] is a 2 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3nw0 3nw0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WY5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WY5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5wy5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3nw0 3nw0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WY5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WY5 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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]] 2.92&#8491;</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=5wy5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wy5 OCA], [http://pdbe.org/5wy5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wy5 RCSB], [http://www.ebi.ac.uk/pdbsum/5wy5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wy5 ProSAT]</span></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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5wy5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wy5 OCA], [https://pdbe.org/5wy5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wy5 RCSB], [https://www.ebi.ac.uk/pdbsum/5wy5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wy5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/NSE3_HUMAN NSE3_HUMAN]] Component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). In vitro enhances ubiquitin ligase activity of NSMCE1. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. May be a growth suppressor that facilitates the entry of the cell into cell cycle arrest.<ref>PMID:20864041</ref> [[http://www.uniprot.org/uniprot/NSE1_HUMAN NSE1_HUMAN]] Component of the SMC5-SMC6 complex, a complex involved in DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). Has in vitro ubiquitin ligase activity in presence of NDNL2. Is involved in positive regulation of response to DNA damage stimulus.<ref>PMID:18086888</ref> <ref>PMID:20864041</ref>
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[https://www.uniprot.org/uniprot/NSE3_HUMAN NSE3_HUMAN] Component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). In vitro enhances ubiquitin ligase activity of NSMCE1. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. May be a growth suppressor that facilitates the entry of the cell into cell cycle arrest.<ref>PMID:20864041</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The melanoma antigen (MAGE) family consists of more than 60 genes, many of which are cancer-testis antigens that are highly expressed in cancer and play a critical role in tumorigenesis. However, the biochemical and cellular functions of this enigmatic family of proteins have remained elusive. Here, we identify really interesting new gene (RING) domain proteins as binding partners for MAGE family proteins. Multiple MAGE family proteins bind E3 RING ubiquitin ligases with specificity. The crystal structure of one of these MAGE-RING complexes, MAGE-G1-NSE1, reveals structural insights into MAGE family proteins and their interaction with E3 RING ubiquitin ligases. Biochemical and cellular assays demonstrate that MAGE proteins enhance the ubiquitin ligase activity of RING domain proteins. For example, MAGE-C2-TRIM28 is shown to target p53 for degradation in a proteasome-dependent manner, consistent with its tumorigenic functions. These findings define a biochemical and cellular function for the MAGE protein family.
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MAGE-RING protein complexes comprise a family of E3 ubiquitin ligases.,Doyle JM, Gao J, Wang J, Yang M, Potts PR Mol Cell. 2010 Sep 24;39(6):963-74. PMID:20864041<ref>PMID:20864041</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5wy5" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Gao, J]]
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[[Category: Homo sapiens]]
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[[Category: Yang, M]]
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[[Category: Large Structures]]
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[[Category: E3 ligase]]
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[[Category: Gao J]]
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[[Category: Metal binding protein]]
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[[Category: Yang M]]
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[[Category: Zn]]
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Current revision

Crystal structure of MAGEG1 and NSE1 complex

PDB ID 5wy5

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