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| | ==DNA binding domain of restriction endonuclease bound to DNA== | | ==DNA binding domain of restriction endonuclease bound to DNA== |
| - | <StructureSection load='3sse' size='340' side='right' caption='[[3sse]], [[Resolution|resolution]] 2.70Å' scene=''> | + | <StructureSection load='3sse' size='340' side='right'caption='[[3sse]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3sse]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SSE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SSE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3sse]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SSE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SSE FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ssc|3ssc]], [[3ssd|3ssd]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ssc|3ssc]], [[3ssd|3ssd]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mcrB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mcrB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=3sse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sse OCA], [http://pdbe.org/3sse PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3sse RCSB], [http://www.ebi.ac.uk/pdbsum/3sse PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3sse 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=3sse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sse OCA], [https://pdbe.org/3sse PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sse RCSB], [https://www.ebi.ac.uk/pdbsum/3sse PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sse ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MCRB_ECOLI MCRB_ECOLI]] Recognizes N4- and C5-methylcytosine (and 5-hydroxy-methylcytosines) produced by a broad range of DNA methylases and appears to act against 5-methylcytosine preceded by a purine residue. Binds to DNA containing methylated cytosines; also binds to GTP. Isoform 33 kDa is less active than isoform 51 kDa and may play a role in regulating the activity of isoform 51 kDa by competing with it in DNA and protein binding abilities. | + | [[https://www.uniprot.org/uniprot/MCRB_ECOLI MCRB_ECOLI]] Recognizes N4- and C5-methylcytosine (and 5-hydroxy-methylcytosines) produced by a broad range of DNA methylases and appears to act against 5-methylcytosine preceded by a purine residue. Binds to DNA containing methylated cytosines; also binds to GTP. Isoform 33 kDa is less active than isoform 51 kDa and may play a role in regulating the activity of isoform 51 kDa by competing with it in DNA and protein binding abilities. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Ecoli]] | | [[Category: Ecoli]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Grazulis, S]] | | [[Category: Grazulis, S]] |
| | [[Category: Siksnys, V]] | | [[Category: Siksnys, V]] |
| Structural highlights
Function
[MCRB_ECOLI] Recognizes N4- and C5-methylcytosine (and 5-hydroxy-methylcytosines) produced by a broad range of DNA methylases and appears to act against 5-methylcytosine preceded by a purine residue. Binds to DNA containing methylated cytosines; also binds to GTP. Isoform 33 kDa is less active than isoform 51 kDa and may play a role in regulating the activity of isoform 51 kDa by competing with it in DNA and protein binding abilities.
Publication Abstract from PubMed
DNA cytosine methylation is a widespread epigenetic mark. Biological effects of DNA methylation are mediated by the proteins that preferentially bind to 5-methylcytosine (5mC) in different sequence contexts. Until now two different structural mechanisms have been established for 5mC recognition in eukaryotes; however, it is still unknown how discrimination of the 5mC modification is achieved in prokaryotes. Here we report the crystal structure of the N-terminal DNA-binding domain (McrB-N) of the methyl-specific endonuclease McrBC from Escherichia coli. The McrB-N protein shows a novel DNA-binding fold adapted for 5mC-recognition. In the McrB-N structure in complex with methylated DNA, the 5mC base is flipped out from the DNA duplex and positioned within a binding pocket. Base flipping elegantly explains why McrBC system restricts only T4-even phages impaired in glycosylation [Luria, S.E. and Human, M.L. (1952) A nonhereditary, host-induced variation of bacterial viruses. J. Bacteriol., 64, 557-569]: flipped out 5-hydroxymethylcytosine is accommodated in the binding pocket but there is no room for the glycosylated base. The mechanism for 5mC recognition employed by McrB-N is highly reminiscent of that for eukaryotic SRA domains, despite the differences in their protein folds.
The recognition domain of the methyl-specific endonuclease McrBC flips out 5-methylcytosine.,Sukackaite R, Grazulis S, Tamulaitis G, Siksnys V Nucleic Acids Res. 2012 May 8. PMID:22570415[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sukackaite R, Grazulis S, Tamulaitis G, Siksnys V. The recognition domain of the methyl-specific endonuclease McrBC flips out 5-methylcytosine. Nucleic Acids Res. 2012 May 8. PMID:22570415 doi:10.1093/nar/gks332
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