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[[Image:1l2c.gif|left|200px]]
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{{STRUCTURE_1l2c|  PDB=1l2c  |  SCENE=  }}
'''MutM (Fpg)-DNA Estranged Thymine Mismatch Recognition Complex'''


==MutM (Fpg)-DNA Estranged Thymine Mismatch Recognition Complex==
<StructureSection load='1l2c' size='340' side='right'caption='[[1l2c]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1l2c]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L2C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L2C 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HPD:1-HYDROXY-PENTANE-3,4-DIOL-5-PHOSPHATE'>HPD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1l2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l2c OCA], [https://pdbe.org/1l2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l2c RCSB], [https://www.ebi.ac.uk/pdbsum/1l2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l2c ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/P84131_GEOSE P84131_GEOSE] Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates (By similarity).[HAMAP-Rule:MF_00103][SAAS:SAAS020629_004_120556]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l2/1l2c_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1l2c ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
MutM is a bacterial 8-oxoguanine glycosylase responsible for initiating base-excision repair of oxidized guanine residues in DNA. Here we report five different crystal structures of MutM-DNA complexes that represent different steps of the repair reaction cascade catalyzed by the protein and also differ in the identity of the base opposite the lesion (the 'estranged' base). These structures reveal that the MutM active site performs the multiple steps of base-excision and 3' and 5' nicking with minimal rearrangement of the DNA backbone.


==Overview==
Structural insights into lesion recognition and repair by the bacterial 8-oxoguanine DNA glycosylase MutM.,Fromme JC, Verdine GL Nat Struct Biol. 2002 Jul;9(7):544-52. PMID:12055620<ref>PMID:12055620</ref>
MutM is a bacterial 8-oxoguanine glycosylase responsible for initiating base-excision repair of oxidized guanine residues in DNA. Here we report five different crystal structures of MutM-DNA complexes that represent different steps of the repair reaction cascade catalyzed by the protein and also differ in the identity of the base opposite the lesion (the 'estranged' base). These structures reveal that the MutM active site performs the multiple steps of base-excision and 3' and 5' nicking with minimal rearrangement of the DNA backbone.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L2C OCA].
</div>
<div class="pdbe-citations 1l2c" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structural insights into lesion recognition and repair by the bacterial 8-oxoguanine DNA glycosylase MutM., Fromme JC, Verdine GL, Nat Struct Biol. 2002 Jul;9(7):544-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12055620 12055620]
*[[DNA glycosylase 3D structures|DNA glycosylase 3D structures]]
[[Category: Fromme, J C.]]
== References ==
[[Category: Verdine, G L.]]
<references/>
[[Category: Dna glycosylase]]
__TOC__
[[Category: Dna repair]]
</StructureSection>
[[Category: Zinc finger]]
[[Category: Geobacillus stearothermophilus]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 23:27:37 2008''
[[Category: Large Structures]]
[[Category: Fromme JC]]
[[Category: Verdine GL]]

Latest revision as of 09:08, 16 August 2023

MutM (Fpg)-DNA Estranged Thymine Mismatch Recognition Complex

1l2c, resolution 2.20Å

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