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7dpd

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Current revision (07:11, 3 April 2024) (edit) (undo)
 
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<StructureSection load='7dpd' size='340' side='right'caption='[[7dpd]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
<StructureSection load='7dpd' size='340' side='right'caption='[[7dpd]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7dpd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DPD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DPD FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7dpd]] is a 2 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=7DPD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DPD FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2.55&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MCM9, C6orf61, MCMDC1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </span></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=7dpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dpd OCA], [https://pdbe.org/7dpd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dpd RCSB], [https://www.ebi.ac.uk/pdbsum/7dpd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dpd 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=7dpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dpd OCA], [https://pdbe.org/7dpd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dpd RCSB], [https://www.ebi.ac.uk/pdbsum/7dpd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dpd ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[https://www.uniprot.org/uniprot/MCM9_HUMAN MCM9_HUMAN]] 46,XX ovarian dysgenesis-short stature syndrome. The disease is caused by variants affecting the gene represented in this entry.
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[https://www.uniprot.org/uniprot/MCM9_HUMAN MCM9_HUMAN] 46,XX ovarian dysgenesis-short stature syndrome. The disease is caused by variants affecting the gene represented in this entry.
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/MCM9_HUMAN MCM9_HUMAN]] Component of the MCM8-MCM9 complex, a complex involved in the repair of double-stranded DNA breaks (DBSs) and DNA interstrand cross-links (ICLs) by homologous recombination (HR) (PubMed:23401855). Required for DNA resection by the MRE11-RAD50-NBN/NBS1 (MRN) complex by recruiting the MRN complex to the repair site and by promoting the complex nuclease activity (PubMed:26215093). Probably by regulating the localization of the MRN complex, indirectly regulates the recruitment of downstream effector RAD51 to DNA damage sites including DBSs and ICLs (PubMed:23401855). Acts as a helicase in DNA mismatch repair (MMR) following DNA replication errors to unwind the mismatch containing DNA strand (PubMed:26300262). In addition, recruits MLH1, a component of the MMR complex, to chromatin (PubMed:26300262). The MCM8-MCM9 complex is dispensable for DNA replication and S phase progression (PubMed:23401855). Probably by regulating HR, plays a key role during gametogenesis (By similarity).[UniProtKB:Q2KHI9]<ref>PMID:23401855</ref> <ref>PMID:26215093</ref> <ref>PMID:26300262</ref>
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[https://www.uniprot.org/uniprot/MCM9_HUMAN MCM9_HUMAN] Component of the MCM8-MCM9 complex, a complex involved in the repair of double-stranded DNA breaks (DBSs) and DNA interstrand cross-links (ICLs) by homologous recombination (HR) (PubMed:23401855). Required for DNA resection by the MRE11-RAD50-NBN/NBS1 (MRN) complex by recruiting the MRN complex to the repair site and by promoting the complex nuclease activity (PubMed:26215093). Probably by regulating the localization of the MRN complex, indirectly regulates the recruitment of downstream effector RAD51 to DNA damage sites including DBSs and ICLs (PubMed:23401855). Acts as a helicase in DNA mismatch repair (MMR) following DNA replication errors to unwind the mismatch containing DNA strand (PubMed:26300262). In addition, recruits MLH1, a component of the MMR complex, to chromatin (PubMed:26300262). The MCM8-MCM9 complex is dispensable for DNA replication and S phase progression (PubMed:23401855). Probably by regulating HR, plays a key role during gametogenesis (By similarity).[UniProtKB:Q2KHI9]<ref>PMID:23401855</ref> <ref>PMID:26215093</ref> <ref>PMID:26300262</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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MCM8/9 is a complex involved in homologous recombination (HR) repair pathway. MCM8/9 dysfunction can cause genome instability and result in primary ovarian insufficiency (POI). However, the mechanism underlying these effects is largely unknown. Here, we report crystal structures of the N-terminal domains (NTDs) of MCM8 and MCM9, and build a ring-shaped NTD structure based on a 6.6 A resolution cryoelectron microscopy map. This shows that the MCM8/9 complex forms a 3:3 heterohexamer in an alternating pattern. A positively charged DNA binding channel and a putative ssDNA exit pathway for fork DNA unwinding are revealed. Based on the atomic model, the potential effects of the clinical POI mutants are interpreted. Surprisingly, the zinc-finger motifs are found to be capable of binding an iron atom as well. Overall, our results provide a model for the formation of the MCM8/9 complex and provide a path for further studies.
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Structural study of the N-terminal domain of human MCM8/9 complex.,Li J, Yu D, Liu L, Liang H, Ouyang Q, Liu Y Structure. 2021 May 22. pii: S0969-2126(21)00164-7. doi:, 10.1016/j.str.2021.05.006. PMID:34043945<ref>PMID:34043945</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 7dpd" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: DNA helicase]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Li, J]]
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[[Category: Li J]]
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[[Category: Liu, L]]
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[[Category: Liu L]]
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[[Category: Liu, Y]]
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[[Category: Liu Y]]
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[[Category: Dna binding]]
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[[Category: Dna binding protein]]
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[[Category: Zinc finger]]
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Current revision

Human MCM9 N-terminal domain

PDB ID 7dpd

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