1aqi

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[[Image:1aqi.gif|left|200px]]
 
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{{Structure
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==STRUCTURE OF ADENINE-N6-DNA-METHYLTRANSFERASE TAQI==
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|PDB= 1aqi |SIZE=350|CAPTION= <scene name='initialview01'>1aqi</scene>, resolution 2.6&Aring;
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<StructureSection load='1aqi' size='340' side='right'caption='[[1aqi]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>
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<table><tr><td colspan='2'>[[1aqi]] is a 2 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=1AQI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AQI FirstGlance]. <br>
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|ACTIVITY= [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]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1aqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aqi OCA], [https://pdbe.org/1aqi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aqi RCSB], [https://www.ebi.ac.uk/pdbsum/1aqi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aqi ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aq/1aqi_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1aqi ConSurf].
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<div style="clear:both"></div>
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'''STRUCTURE OF ADENINE-N6-DNA-METHYLTRANSFERASE TAQI'''
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==See Also==
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*[[DNA methyltransferase 3D structures|DNA methyltransferase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The crystal structures of the binary complexes of the DNA methyltransferase M.TaqI with the inhibitor Sinefungin and the reaction product S-adenosyl-L-homocysteine were determined, both at 2.6 A resolution. Structural comparison of these binary complexes with the complex formed by M.TaqI and the cofactor S-adenosyl-L-methionine suggests that the key element for molecular recognition of these ligands is the binding of their adenosine part in a pocket, and discrimination between cofactor, reaction product and inhibitor is mediated by different conformations of these molecules; the methionine part of S-adenosyl-L-methionine is located in the binding cleft, whereas the amino acid moieties of Sinefungin and S-adenosyl-L-homocysteine are in a different orientation and interact with the active site amino acid residues 105NPPY108. Dissociation constants for the complexes of M.TaqI with the three ligands were determined spectrofluorometrically. Sinefungin binds more strongly than S-adenosyl-L-homocysteine or S-adenosyl-L-methionine, with KD=0.34 microM, 2.4 microM and 2.0 microM, respectively.
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[[Category: Large Structures]]
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==About this Structure==
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1AQI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AQI OCA].
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==Reference==
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Differential binding of S-adenosylmethionine S-adenosylhomocysteine and Sinefungin to the adenine-specific DNA methyltransferase M.TaqI., Schluckebier G, Kozak M, Bleimling N, Weinhold E, Saenger W, J Mol Biol. 1997 Jan 10;265(1):56-67. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8995524 8995524]
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[[Category: Single protein]]
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[[Category: Site-specific DNA-methyltransferase (adenine-specific)]]
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[[Category: Thermus aquaticus]]
[[Category: Thermus aquaticus]]
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[[Category: Saenger, W.]]
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[[Category: Saenger W]]
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[[Category: Schluckebier, G.]]
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[[Category: Schluckebier G]]
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[[Category: SAH]]
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[[Category: methyltransferase]]
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[[Category: restriction system]]
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[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:01:02 2008''
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Current revision

STRUCTURE OF ADENINE-N6-DNA-METHYLTRANSFERASE TAQI

PDB ID 1aqi

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