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| | ==Crystal structure of mouse Morc3 ATPase-CW cassette in complex with AMPPNP and H3K4me3 peptide== | | ==Crystal structure of mouse Morc3 ATPase-CW cassette in complex with AMPPNP and H3K4me3 peptide== |
| - | <StructureSection load='5ix1' size='340' side='right' caption='[[5ix1]], [[Resolution|resolution]] 2.60Å' scene=''> | + | <StructureSection load='5ix1' size='340' side='right'caption='[[5ix1]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ix1]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IX1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IX1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ix1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IX1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IX1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ix2|5ix2]]</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=5ix1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ix1 OCA], [https://pdbe.org/5ix1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ix1 RCSB], [https://www.ebi.ac.uk/pdbsum/5ix1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ix1 ProSAT]</span></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=5ix1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ix1 OCA], [http://pdbe.org/5ix1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ix1 RCSB], [http://www.ebi.ac.uk/pdbsum/5ix1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ix1 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MORC3_MOUSE MORC3_MOUSE]] Nuclear factor which forms MORC3-NBs (nuclear bodies) via an ATP-dependent mechanism (By similarity). Sumoylated MORC3-NBs can also associate with PML-NBs (By similarity). Recruits TP53 and SP100 to PML-NBs, thus regulating TP53 activity (PubMed:17332504). Binds RNA in vitro (By similarity).[UniProtKB:Q14149]<ref>PMID:17332504</ref> | + | [https://www.uniprot.org/uniprot/MORC3_MOUSE MORC3_MOUSE] Nuclear factor which forms MORC3-NBs (nuclear bodies) via an ATP-dependent mechanism (By similarity). Sumoylated MORC3-NBs can also associate with PML-NBs (By similarity). Recruits TP53 and SP100 to PML-NBs, thus regulating TP53 activity (PubMed:17332504). Binds RNA in vitro (By similarity).[UniProtKB:Q14149]<ref>PMID:17332504</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Du, J]] | + | [[Category: Large Structures]] |
| - | [[Category: Li, S]] | + | [[Category: Mus musculus]] |
| - | [[Category: Patel, D J]] | + | [[Category: Du J]] |
| - | [[Category: Atpase]] | + | [[Category: Li S]] |
| - | [[Category: Cw domain]] | + | [[Category: Patel DJ]] |
| - | [[Category: H3k4me3]]
| + | |
| - | [[Category: Morc3]]
| + | |
| - | [[Category: Transcription]]
| + | |
| Structural highlights
Function
MORC3_MOUSE Nuclear factor which forms MORC3-NBs (nuclear bodies) via an ATP-dependent mechanism (By similarity). Sumoylated MORC3-NBs can also associate with PML-NBs (By similarity). Recruits TP53 and SP100 to PML-NBs, thus regulating TP53 activity (PubMed:17332504). Binds RNA in vitro (By similarity).[UniProtKB:Q14149][1]
Publication Abstract from PubMed
Microrchidia (MORC) proteins are GHKL (gyrase, heat-shock protein 90, histidine kinase, MutL) ATPases that function in gene regulation in multiple organisms. Animal MORCs also contain CW-type zinc finger domains, which are known to bind to modified histones. We solved the crystal structure of the murine MORC3 ATPase-CW domain bound to the nucleotide analog AMPPNP (phosphoaminophosphonic acid-adenylate ester) and in complex with a trimethylated histone H3 lysine 4 (H3K4) peptide (H3K4me3). We observed that the MORC3 N-terminal ATPase domain forms a dimer when bound to AMPPNP. We used native mass spectrometry to show that dimerization is ATP-dependent, and that dimer formation is enhanced in the presence of nonhydrolyzable ATP analogs. The CW domain uses an aromatic cage to bind trimethylated Lys4 and forms extensive hydrogen bonds with the H3 tail. We found that MORC3 localizes to promoters marked by H3K4me3 throughout the genome, consistent with its binding to H3K4me3 in vitro. Our work sheds light on aspects of the molecular dynamics and function of MORC3.
Mouse MORC3 is a GHKL ATPase that localizes to H3K4me3 marked chromatin.,Li S, Yen L, Pastor WA, Johnston JB, Du J, Shew CJ, Liu W, Ho J, Stender B, Clark AT, Burlingame AL, Daxinger L, Patel DJ, Jacobsen SE Proc Natl Acad Sci U S A. 2016 Aug 30;113(35):E5108-16. doi:, 10.1073/pnas.1609709113. Epub 2016 Aug 15. PMID:27528681[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Takahashi K, Yoshida N, Murakami N, Kawata K, Ishizaki H, Tanaka-Okamoto M, Miyoshi J, Zinn AR, Shime H, Inoue N. Dynamic regulation of p53 subnuclear localization and senescence by MORC3. Mol Biol Cell. 2007 May;18(5):1701-9. Epub 2007 Mar 1. PMID:17332504 doi:http://dx.doi.org/10.1091/mbc.E06-08-0747
- ↑ Li S, Yen L, Pastor WA, Johnston JB, Du J, Shew CJ, Liu W, Ho J, Stender B, Clark AT, Burlingame AL, Daxinger L, Patel DJ, Jacobsen SE. Mouse MORC3 is a GHKL ATPase that localizes to H3K4me3 marked chromatin. Proc Natl Acad Sci U S A. 2016 Aug 30;113(35):E5108-16. doi:, 10.1073/pnas.1609709113. Epub 2016 Aug 15. PMID:27528681 doi:http://dx.doi.org/10.1073/pnas.1609709113
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