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| ==MspJI Restriction Endonuclease - P21 Form== | | ==MspJI Restriction Endonuclease - P21 Form== |
| <StructureSection load='4f0q' size='340' side='right' caption='[[4f0q]], [[Resolution|resolution]] 2.05Å' scene=''> | | <StructureSection load='4f0q' size='340' side='right'caption='[[4f0q]], [[Resolution|resolution]] 2.05Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[4f0q]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycsj Mycsj]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F0Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F0Q FirstGlance]. <br> | | <table><tr><td colspan='2'>[[4f0q]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_sp._JLS Mycobacterium sp. JLS]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F0Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F0Q FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.046Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4f0p|4f0p]]</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Mjls_0822 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=164757 MYCSJ])</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=4f0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f0q OCA], [https://pdbe.org/4f0q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f0q RCSB], [https://www.ebi.ac.uk/pdbsum/4f0q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f0q 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=4f0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f0q OCA], [http://pdbe.org/4f0q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4f0q RCSB], [http://www.ebi.ac.uk/pdbsum/4f0q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4f0q ProSAT]</span></td></tr> | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/A0A0J9X157_MYCSJ A0A0J9X157_MYCSJ] |
| The MspJI modification-dependent restriction endonuclease recognizes 5-methylcytosine or 5-hydroxymethylcytosine in the context of CNN(G/A) and cleaves both strands at fixed distances (N(12)/N(16)) away from the modified cytosine at the 3'-side. We determined the crystal structure of MspJI of Mycobacterium sp. JLS at 2.05-A resolution. Each protein monomer harbors two domains: an N-terminal DNA-binding domain and a C-terminal endonuclease. The N-terminal domain is structurally similar to that of the eukaryotic SET and RING-associated domain, which is known to bind to a hemi-methylated CpG dinucleotide. Four protein monomers are found in the crystallographic asymmetric unit. Analytical gel-filtration and ultracentrifugation measurements confirm that the protein exists as a tetramer in solution. Two monomers form a back-to-back dimer mediated by their C-terminal endonuclease domains. Two back-to-back dimers interact to generate a tetramer with two double-stranded DNA cleavage modules. Each cleavage module contains two active sites facing each other, enabling double-strand DNA cuts. Biochemical, mutagenesis and structural characterization suggest three different monomers of the tetramer may be involved respectively in binding the modified cytosine, making the first proximal N(12) cleavage in the same strand and then the second distal N(16) cleavage in the opposite strand. Both cleavage events require binding of at least a second recognition site either in cis or in trans.
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| Structure and cleavage activity of the tetrameric MspJI DNA modification-dependent restriction endonuclease.,Horton JR, Mabuchi MY, Cohen-Karni D, Zhang X, Griggs RM, Samaranayake M, Roberts RJ, Zheng Y, Cheng X Nucleic Acids Res. 2012 Jul 30. PMID:22848107<ref>PMID:22848107</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 4f0q" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Mycsj]] | | [[Category: Large Structures]] |
| [[Category: Cheng, X]] | | [[Category: Mycobacterium sp. JLS]] |
| [[Category: Cohen-Karni, D]] | | [[Category: Cheng X]] |
| [[Category: Griggs, R]] | | [[Category: Cohen-Karni D]] |
| [[Category: Horton, J R]] | | [[Category: Griggs R]] |
| [[Category: Mabuchi, M]] | | [[Category: Horton JR]] |
| [[Category: Roberts, R J]] | | [[Category: Mabuchi M]] |
| [[Category: Samaranayake, M]] | | [[Category: Roberts RJ]] |
| [[Category: Zhang, X]] | | [[Category: Samaranayake M]] |
| [[Category: Zheng, Y]] | | [[Category: Zhang X]] |
| [[Category: Cytosine methylation-dependent endonuclease]]
| | [[Category: Zheng Y]] |
| [[Category: Hydrolase]]
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