2ih5: Difference between revisions

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[[Image:2ih5.gif|left|200px]]<br /><applet load="2ih5" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2ih5, resolution 1.80&Aring;" />
'''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'''<br />


==About this Structure==
==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 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus] with <scene name='pdbligand=NEA:'>NEA</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Site-specific_DNA-methyltransferase_(adenine-specific) Site-specific DNA-methyltransferase (adenine-specific)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.72 2.1.1.72] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IH5 OCA].  
<StructureSection load='2ih5' size='340' side='right'caption='[[2ih5]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
[[Category: Single protein]]
== Structural highlights ==
[[Category: Site-specific DNA-methyltransferase (adenine-specific)]]
<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='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='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='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>
== 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.
== 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/ih/2ih5_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=2ih5 ConSurf].
<div style="clear:both"></div>
 
==See Also==
*[[DNA methyltransferase 3D structures|DNA methyltransferase 3D structures]]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermus aquaticus]]
[[Category: Thermus aquaticus]]
[[Category: Lenz, T.]]
[[Category: Lenz T]]
[[Category: Scheidig, A J.]]
[[Category: Scheidig AJ]]
[[Category: Weinhold, E.]]
[[Category: Weinhold E]]
[[Category: GOL]]
[[Category: NEA]]
[[Category: abasic site analog]]
[[Category: base flipping]]
[[Category: dna]]
[[Category: dna methyltransferase]]
[[Category: nucleotide flipping]]
[[Category: target base partner]]
[[Category: transferase/dna complex]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:52:40 2008''

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 an abasic site analog 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 an abasic site analog at the target base partner position

Structural highlights

2ih5 is a 3 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 1.8Å
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

2ih5, resolution 1.80Å

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