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2adm

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[[Image:2adm.jpg|left|200px]]
 
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==ADENINE-N6-DNA-METHYLTRANSFERASE TAQI==
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The line below this paragraph, containing "STRUCTURE_2adm", creates the "Structure Box" on the page.
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<StructureSection load='2adm' size='340' side='right'caption='[[2adm]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2adm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1adm 1adm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ADM FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
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{{STRUCTURE_2adm| PDB=2adm | SCENE= }}
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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=2adm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2adm OCA], [https://pdbe.org/2adm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2adm RCSB], [https://www.ebi.ac.uk/pdbsum/2adm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2adm 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/ad/2adm_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=2adm ConSurf].
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<div style="clear:both"></div>
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'''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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2ADM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1adm 1adm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADM 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: 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: 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 Sat May 3 18:54:55 2008''
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Current revision

ADENINE-N6-DNA-METHYLTRANSFERASE TAQI

PDB ID 2adm

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