2ih2: Difference between revisions

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<StructureSection load='2ih2' size='340' side='right'caption='[[2ih2]], [[Resolution|resolution]] 1.61&Aring;' scene=''>
<StructureSection load='2ih2' size='340' side='right'caption='[[2ih2]], [[Resolution|resolution]] 1.61&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2ih2]] is a 6 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=2IH2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IH2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2ih2]] is a 6 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=2IH2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IH2 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]] 1.61&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=5PY:1-(2-DEOXY-5-O-PHOSPHONO-BETA-D-ERYTHRO-PENTOFURANOSYL)-5-METHYLPYRIMIDIN-2(1H)-ONE'>5PY</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=5PY:1-(2-DEOXY-5-O-PHOSPHONO-BETA-D-ERYTHRO-PENTOFURANOSYL)-5-METHYLPYRIMIDIN-2(1H)-ONE'>5PY</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]], [[2ih4|2ih4]], [[2ih5|2ih5]]</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=2ih2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ih2 OCA], [https://pdbe.org/2ih2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ih2 RCSB], [https://www.ebi.ac.uk/pdbsum/2ih2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ih2 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=2ih2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ih2 OCA], [https://pdbe.org/2ih2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ih2 RCSB], [https://www.ebi.ac.uk/pdbsum/2ih2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ih2 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: Base flipping]]
[[Category: Weinhold E]]
[[Category: Dna]]
[[Category: Dna methyltransferase]]
[[Category: Nucleotide flipping]]
[[Category: Target base partner]]
[[Category: Transferase-dna complex]]

Latest revision as of 13:11, 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 5-methylpyrimidin-2(1H)-one at the target base partner positionCrystal structure of the adenine-specific DNA methyltransferase M.TaqI complexed with the cofactor analog AETA and a 10 bp DNA containing 5-methylpyrimidin-2(1H)-one at the target base partner position

Structural highlights

2ih2 is a 6 chain structure with sequence from Thermus aquaticus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.61Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2ih2, resolution 1.61Å

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