4ea5: Difference between revisions

Latest revision as of 17:56, 14 March 2024

Structure of the glycoslyase domain of MBD4 bound to a 5hmU containing DNAStructure of the glycoslyase domain of MBD4 bound to a 5hmU containing DNA

Structural highlights

4ea5 is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.14Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MBD4_HUMAN Mismatch-specific DNA N-glycosylase involved in DNA repair. Has thymine glycosylase activity and is specific for G:T mismatches within methylated and unmethylated CpG sites. Can also remove uracil or 5-fluorouracil in G:U mismatches. Has no lyase activity. Was first identified as methyl-CpG-binding protein.^[1] ^[2]

References

↑ Bellacosa A, Cicchillitti L, Schepis F, Riccio A, Yeung AT, Matsumoto Y, Golemis EA, Genuardi M, Neri G. MED1, a novel human methyl-CpG-binding endonuclease, interacts with DNA mismatch repair protein MLH1. Proc Natl Acad Sci U S A. 1999 Mar 30;96(7):3969-74. PMID:10097147
↑ Petronzelli F, Riccio A, Markham GD, Seeholzer SH, Stoerker J, Genuardi M, Yeung AT, Matsumoto Y, Bellacosa A. Biphasic kinetics of the human DNA repair protein MED1 (MBD4), a mismatch-specific DNA N-glycosylase. J Biol Chem. 2000 Oct 20;275(42):32422-9. PMID:10930409 doi:10.1074/jbc.M004535200

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OCA

[1] Bellacosa A, Cicchillitti L, Schepis F, Riccio A, Yeung AT, Matsumoto Y, Golemis EA, Genuardi M, Neri G. MED1, a novel human methyl-CpG-binding endonuclease, interacts with DNA mismatch repair protein MLH1. Proc Natl Acad Sci U S A. 1999 Mar 30;96(7):3969-74. PMID:10097147

[2] Petronzelli F, Riccio A, Markham GD, Seeholzer SH, Stoerker J, Genuardi M, Yeung AT, Matsumoto Y, Bellacosa A. Biphasic kinetics of the human DNA repair protein MED1 (MBD4), a mismatch-specific DNA N-glycosylase. J Biol Chem. 2000 Oct 20;275(42):32422-9. PMID:10930409 doi:10.1074/jbc.M004535200

[1]

[2]

@@ Line 1: / Line 1: @@
-[[Image:4ea5.jpg|left|200px]]
-{{STRUCTURE_4ea5|  PDB=4ea5  |  SCENE=  }}
+==Structure of the glycoslyase domain of MBD4 bound to a 5hmU containing DNA==
+<StructureSection load='4ea5' size='340' side='right'caption='[[4ea5]], [[Resolution|resolution]] 2.14&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4ea5]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EA5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EA5 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.14&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5HU:5-HYDROXYMETHYLURIDINE-2-DEOXY-5-MONOPHOSPHATE'>5HU</scene></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=4ea5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ea5 OCA], [https://pdbe.org/4ea5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ea5 RCSB], [https://www.ebi.ac.uk/pdbsum/4ea5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ea5 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MBD4_HUMAN MBD4_HUMAN] Mismatch-specific DNA N-glycosylase involved in DNA repair. Has thymine glycosylase activity and is specific for G:T mismatches within methylated and unmethylated CpG sites. Can also remove uracil or 5-fluorouracil in G:U mismatches. Has no lyase activity. Was first identified as methyl-CpG-binding protein.<ref>PMID:10097147</ref> <ref>PMID:10930409</ref>
-===Structure of the glycoslyase domain of MBD4 bound to a 5hmU containing DNA===
+==See Also==
+*[[Methyl CpG binding protein 3D structures|Methyl CpG binding protein 3D structures]]
-{{ABSTRACT_PUBMED_22848106}}
+== References ==
+<references/>
-==About this Structure==
+__TOC__
-[[4ea5]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EA5 OCA].
+</StructureSection>
-==Reference==
-<ref group="xtra">PMID:022848106</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Morera, S.]]
+[[Category: Large Structures]]
-[[Category: Vigouroux, A.]]
+[[Category: Morera S]]
-[[Category: Hhh dna glycosylase family]]
+[[Category: Vigouroux A]]
-[[Category: Hydrolase-dna complex]]

4ea5: Difference between revisions

Latest revision as of 17:56, 14 March 2024

Structure of the glycoslyase domain of MBD4 bound to a 5hmU containing DNAStructure of the glycoslyase domain of MBD4 bound to a 5hmU containing DNA

Structural highlights

Function

See Also

References

Contents

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4ea5: Difference between revisions

Latest revision as of 17:56, 14 March 2024

Structure of the glycoslyase domain of MBD4 bound to a 5hmU containing DNAStructure of the glycoslyase domain of MBD4 bound to a 5hmU containing DNA

Structural highlights

Function

See Also

References

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

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