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6gcf
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==DNA binding domain of restriction endonuclease McrBC in complex with N4-methylcytosine DNA== | |
| + | <StructureSection load='6gcf' size='340' side='right' caption='[[6gcf]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6gcf]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GCF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GCF FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=C34:N4-METHYL-2-DEOXY-CYTIDINE-5-MONOPHOSPHATE'>C34</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6gcd|6gcd]], [[6gce|6gce]]</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=6gcf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gcf OCA], [http://pdbe.org/6gcf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gcf RCSB], [http://www.ebi.ac.uk/pdbsum/6gcf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gcf ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cytosine modifications expand the information content of genomic DNA in both eukaryotes and prokaryotes, providing means for epigenetic regulation and self versus non-self discrimination. For example, the methyl-directed restriction endonuclease McrBC recognizes and cuts invading bacteriophage DNA containing 5-methylcytosine (5mC), 5-hydroxymethylcytosine (5hmC) and N4-methylcytosine (4mC), leaving unmodified host DNA intact. Here, we present co-crystal structures of McrB-N bound to DNA oligoduplexes containing 5hmC, 5-formylcytosine (5fC) and 4mC, and characterise the relative affinity of McrB-N to various cytosine variants. We find that McrB-N flips out modified bases into a protein pocket and binds cytosine derivatives in the order of descending affinity: 4mC>5mC>5hmC>>5fC. We also show that pocket mutations alter the relative preference of McrB-N to 5mC, 5hmC and 4mC. This article is protected by copyright. All rights reserved. | ||
| - | + | Recognition of modified cytosine variants by the DNA binding domain of methyl-directed endonuclease McrBC.,Zagorskaite E, Manakova E, Sasnauskas G FEBS Lett. 2018 Sep 8. doi: 10.1002/1873-3468.13244. PMID:30194838<ref>PMID:30194838</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6gcf" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Sasnauskas, G]] | ||
| + | [[Category: Base flipping]] | ||
| + | [[Category: Dna binding protein]] | ||
| + | [[Category: Mcrbc]] | ||
| + | [[Category: N4-methylcytosine]] | ||
| + | [[Category: Restriction endonuclease]] | ||
Revision as of 19:55, 19 September 2018
DNA binding domain of restriction endonuclease McrBC in complex with N4-methylcytosine DNA
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