4ofh: Difference between revisions

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'''Unreleased structure'''
==Structural basis for thymine glycosylase activity on T:O6-methylG mismatch by methyl-CpG binding domain protein 4: Implications for roles of Arg468 in mismatch recognition and catalysis==
 
<StructureSection load='4ofh' size='340' side='right' caption='[[4ofh]], [[Resolution|resolution]] 2.22&Aring;' scene=''>
The entry 4ofh is ON HOLD  until Apr 22 2016
== Structural highlights ==
 
<table><tr><td colspan='2'>[[4ofh]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OFH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OFH FirstGlance]. <br>
Authors: Ouzon-Shubeita, H., Lin, Y.-L., Lee, S.
</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>
 
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=6OG:6-O-METHYL+GUANOSINE-5-MONOPHOSPHATE'>6OG</scene></td></tr>
Description: Structural basis for thymine glycosylase activity on T:O6-methylG mismatch by methyl-CpG binding domain protein 4: Implications for roles of Arg468 in mismatch recognition and catalysis
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3iho|3iho]], [[4ea5|4ea5]], [[4e9g|4e9g]], [[4e9e|4e9e]], [[4e9f|4e9f]], [[4ea4|4ea4]], [[4ofa|4ofa]], [[4ofe|4ofe]]</td></tr>
[[Category: Unreleased Structures]]
<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=4ofh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ofh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ofh RCSB], [http://www.ebi.ac.uk/pdbsum/4ofh PDBsum]</span></td></tr>
[[Category: Lin, Y.-L]]
</table>
== Function ==
[[http://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> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Lee, S]]
[[Category: Lin, Y L]]
[[Category: Ouzon-Shubeita, H]]
[[Category: Ouzon-Shubeita, H]]
[[Category: Lee, S]]
[[Category: Hydrolase-dna complex]]
[[Category: Mismatch]]
[[Category: Protein-dna complex]]
[[Category: Thymine glycosylase]]

Revision as of 15:51, 22 April 2015

Structural basis for thymine glycosylase activity on T:O6-methylG mismatch by methyl-CpG binding domain protein 4: Implications for roles of Arg468 in mismatch recognition and catalysisStructural basis for thymine glycosylase activity on T:O6-methylG mismatch by methyl-CpG binding domain protein 4: Implications for roles of Arg468 in mismatch recognition and catalysis

Structural highlights

4ofh is a 3 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Resources:FirstGlance, OCA, RCSB, PDBsum

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

  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

4ofh, resolution 2.22Å

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