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5wy1

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Revision as of 07:19, 7 October 2020

Crystal structure of mouse DNA methyltransferase 1 (T1505A mutant)

Structural highlights

5wy1 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:	DNA (cytosine-5-)-methyltransferase, with EC number 2.1.1.37
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DNMT1_MOUSE] Methylates CpG residues. Preferentially methylates hemimethylated DNA. Associates with DNA replication sites in S phase maintaining the methylation pattern in the newly synthesized strand, that is essential for epigenetic inheritance. Associates with chromatin during G2 and M phases to maintain DNA methylation independently of replication. It is responsible for maintaining methylation patterns established in development. DNA methylation is coordinated with methylation of histones. Mediates transcriptional repression by direct binding to HDAC2. In association with DNMT3B and via the recruitment of CTCFL/BORIS, involved in activation of BAG1 gene expression by modulating dimethylation of promoter histone H3 at H3K4 and H3K9.^[1] ^[2] ^[3]

Publication Abstract from PubMed

In mammals, DNA methyltransferase 1 (DNMT1) is responsible for propagating the DNA methylation pattern into the next generation through selective methylation of hemi-methylated CpG that emerges just after replication, a process known as maintenance methylation. The T1505, which is conserved among DNMT1s of vertebrates, in the catalytic domain of mouse DNMT1 forms the hydrogen bond with the W1512, which is also conserved among vertebrates and one of the essential residues in recognition of the 5-methylcytosine in hemi-methylated CpGs. However, importance of the hydrogen bond between T1505 and W1512 is unknown. In this study, we determined the crystal structure of mouse DNMT1(291-1620) that replaced T1505 with alanine (DNMT1(291-1620)T1505A) and examined its DNA methylation activity in vitro. Although the mutation lost the hydrogen bond between T1505 and W1512, the overall structure of DNMT1(291-1620)T1505A remained almost identical with that of the wild type. Structural stability and DNA methylation activity of DNMT1(291-1620)T1505A under physiological temperature were lower than those of DNMT1(291-1620). T1505 is crucial on the DNA methylation activity of DNMT1 through stabilizing its structure during ongoing round of DNA methylation.

Conserved threonine 1505 in the catalytic domain stabilizes mouse DNA methyltransferase 1.,Kanada K, Takeshita K, Suetake I, Tajima S, Nakagawa A J Biochem. 2017 Mar 24. doi: 10.1093/jb/mvx024. PMID:28369487^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Howell CY, Bestor TH, Ding F, Latham KE, Mertineit C, Trasler JM, Chaillet JR. Genomic imprinting disrupted by a maternal effect mutation in the Dnmt1 gene. Cell. 2001 Mar 23;104(6):829-38. PMID:11290321
↑ Easwaran HP, Schermelleh L, Leonhardt H, Cardoso MC. Replication-independent chromatin loading of Dnmt1 during G2 and M phases. EMBO Rep. 2004 Dec;5(12):1181-6. PMID:15550930 doi:http://dx.doi.org/10.1038/sj.embor.7400295
↑ Schermelleh L, Haemmer A, Spada F, Rosing N, Meilinger D, Rothbauer U, Cardoso MC, Leonhardt H. Dynamics of Dnmt1 interaction with the replication machinery and its role in postreplicative maintenance of DNA methylation. Nucleic Acids Res. 2007;35(13):4301-12. Epub 2007 Jun 18. PMID:17576694 doi:http://dx.doi.org/10.1093/nar/gkm432
↑ Kanada K, Takeshita K, Suetake I, Tajima S, Nakagawa A. Conserved threonine 1505 in the catalytic domain stabilizes mouse DNA methyltransferase 1. J Biochem. 2017 Mar 24. doi: 10.1093/jb/mvx024. PMID:28369487 doi:http://dx.doi.org/10.1093/jb/mvx024

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5wy1"

@@ Line 1: / Line 1: @@
 ==Crystal structure of mouse DNA methyltransferase 1 (T1505A mutant)==
-<StructureSection load='5wy1' size='340' side='right' caption='[[5wy1]], [[Resolution|resolution]] 3.27&Aring;' scene=''>
+<StructureSection load='5wy1' size='340' side='right'caption='[[5wy1]], [[Resolution|resolution]] 3.27&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5wy1]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WY1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WY1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5wy1]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WY1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5WY1 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_(cytosine-5-)-methyltransferase DNA (cytosine-5-)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.37 2.1.1.37] </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=5wy1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wy1 OCA], [http://pdbe.org/5wy1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wy1 RCSB], [http://www.ebi.ac.uk/pdbsum/5wy1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wy1 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5wy1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wy1 OCA], [http://pdbe.org/5wy1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wy1 RCSB], [http://www.ebi.ac.uk/pdbsum/5wy1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wy1 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 19: / Line 19: @@
 </div>
 <div class="pdbe-citations 5wy1" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[DNA methyltransferase 3D structures|DNA methyltransferase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Kanada, K]]
 [[Category: Nakagawa, A]]

5wy1

From Proteopedia

Revision as of 07:19, 7 October 2020

Crystal structure of mouse DNA methyltransferase 1 (T1505A mutant)

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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