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< | ==Crystal structure of MutH-hemimethylated DNA complex== | ||
<StructureSection load='2aor' size='340' side='right'caption='[[2aor]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2aor]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AOR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AOR FirstGlance]. <br> | |||
or | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6MA:N6-METHYL-DEOXY-ADENOSINE-5-MONOPHOSPHATE'>6MA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=2aor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aor OCA], [https://pdbe.org/2aor PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2aor RCSB], [https://www.ebi.ac.uk/pdbsum/2aor PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2aor ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/MUTH_HAEIN MUTH_HAEIN] Sequence-specific endonuclease that cleaves unmethylated GATC sequences. It is involved in DNA mismatch repair (By similarity). | |||
== 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/ao/2aor_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=2aor ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
MutH initiates mismatch repair by nicking the transiently unmethylated daughter strand 5' to a GATC sequence. Here, we report crystal structures of MutH complexed with hemimethylated and unmethylated GATC substrates. Both structures contain two Ca2+ ions jointly coordinated by a conserved aspartate and the scissile phosphate, as observed in the restriction endonucleases BamHI and BglI. In the hemimethylated complexes, the active site is more compact and DNA cleavage is more efficient. The Lys residue in the conserved DEK motif coordinates the nucleophilic water in conjunction with the phosphate 3' to the scissile bond; the same Lys is also hydrogen bonded with a carbonyl oxygen in the DNA binding module. We propose that this Lys, which is conserved in many restriction endonucleases and is replaced by Glu or Gln in BamHI and BglII, is a sensor for DNA binding and the linchpin that couples base recognition and DNA cleavage. | |||
MutH complexed with hemi- and unmethylated DNAs: coupling base recognition and DNA cleavage.,Lee JY, Chang J, Joseph N, Ghirlando R, Rao DN, Yang W Mol Cell. 2005 Oct 7;20(1):155-66. PMID:16209953<ref>PMID:16209953</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2aor" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[DNA mismatch repair protein 3D structures|DNA mismatch repair protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
== | |||
< | |||
[[Category: Haemophilus influenzae]] | [[Category: Haemophilus influenzae]] | ||
[[Category: Chang | [[Category: Large Structures]] | ||
[[Category: Ghirlando | [[Category: Chang J]] | ||
[[Category: Joseph | [[Category: Ghirlando R]] | ||
[[Category: Lee | [[Category: Joseph N]] | ||
[[Category: Rao | [[Category: Lee JY]] | ||
[[Category: Yang | [[Category: Rao DN]] | ||
[[Category: Yang W]] | |||
Latest revision as of 10:27, 23 August 2023
Crystal structure of MutH-hemimethylated DNA complexCrystal structure of MutH-hemimethylated DNA complex
Structural highlights
FunctionMUTH_HAEIN Sequence-specific endonuclease that cleaves unmethylated GATC sequences. It is involved in DNA mismatch repair (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMutH initiates mismatch repair by nicking the transiently unmethylated daughter strand 5' to a GATC sequence. Here, we report crystal structures of MutH complexed with hemimethylated and unmethylated GATC substrates. Both structures contain two Ca2+ ions jointly coordinated by a conserved aspartate and the scissile phosphate, as observed in the restriction endonucleases BamHI and BglI. In the hemimethylated complexes, the active site is more compact and DNA cleavage is more efficient. The Lys residue in the conserved DEK motif coordinates the nucleophilic water in conjunction with the phosphate 3' to the scissile bond; the same Lys is also hydrogen bonded with a carbonyl oxygen in the DNA binding module. We propose that this Lys, which is conserved in many restriction endonucleases and is replaced by Glu or Gln in BamHI and BglII, is a sensor for DNA binding and the linchpin that couples base recognition and DNA cleavage. MutH complexed with hemi- and unmethylated DNAs: coupling base recognition and DNA cleavage.,Lee JY, Chang J, Joseph N, Ghirlando R, Rao DN, Yang W Mol Cell. 2005 Oct 7;20(1):155-66. PMID:16209953[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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