2ih5: Difference between revisions

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<StructureSection load='2ih5' size='340' side='right'caption='[[2ih5]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='2ih5' size='340' side='right'caption='[[2ih5]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2ih5]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_25104 Atcc 25104]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IH5 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2ih5]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IH5 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NEA:5-DEOXY-5-[2-(AMINO)ETHYLTHIO]ADENOSINE'>NEA</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=3DR:1,2-DIDEOXYRIBOFURANOSE-5-PHOSPHATE'>3DR</scene>, <scene name='pdbligand=6MA:N6-METHYL-DEOXY-ADENOSINE-5-MONOPHOSPHATE'>6MA</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3DR:1,2-DIDEOXYRIBOFURANOSE-5-PHOSPHATE'>3DR</scene>, <scene name='pdbligand=6MA:N6-METHYL-DEOXY-ADENOSINE-5-MONOPHOSPHATE'>6MA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NEA:5-DEOXY-5-[2-(AMINO)ETHYLTHIO]ADENOSINE'>NEA</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1g38|1g38]], [[2adm|2adm]], [[1aqi|1aqi]], [[1aqj|1aqj]], [[2ibs|2ibs]], [[2ibt|2ibt]], [[2ih2|2ih2]], [[2ih4|2ih4]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">taqIM ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=271 ATCC 25104])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Site-specific_DNA-methyltransferase_(adenine-specific) Site-specific DNA-methyltransferase (adenine-specific)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.72 2.1.1.72] </span></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=2ih5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ih5 OCA], [https://pdbe.org/2ih5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ih5 RCSB], [https://www.ebi.ac.uk/pdbsum/2ih5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ih5 ProSAT]</span></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=2ih5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ih5 OCA], [https://pdbe.org/2ih5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ih5 RCSB], [https://www.ebi.ac.uk/pdbsum/2ih5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ih5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/MTTA_THEAQ MTTA_THEAQ]] This methylase recognizes the double-stranded sequence TCGA, causes specific methylation on A-4 on both strands and protects the DNA from cleavage by the TaqI endonuclease.  
[https://www.uniprot.org/uniprot/MTTA_THEAQ MTTA_THEAQ] This methylase recognizes the double-stranded sequence TCGA, causes specific methylation on A-4 on both strands and protects the DNA from cleavage by the TaqI endonuclease.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 25104]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lenz, T]]
[[Category: Thermus aquaticus]]
[[Category: Scheidig, A J]]
[[Category: Lenz T]]
[[Category: Weinhold, E]]
[[Category: Scheidig AJ]]
[[Category: Abasic site analog]]
[[Category: Weinhold E]]
[[Category: Base flipping]]
[[Category: Dna]]
[[Category: Dna methyltransferase]]
[[Category: Nucleotide flipping]]
[[Category: Target base partner]]
[[Category: Transferase-dna complex]]

Latest revision as of 10:11, 30 August 2023

Crystal structure of the adenine-specific DNA methyltransferase M.TaqI complexed with the cofactor analog AETA and a 10 bp DNA containing an abasic site analog at the target base partner position

2ih5, resolution 1.80Å

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