2adm: Difference between revisions

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OCA

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-[[Image:2adm.jpg|left|200px]]<br /><applet load="2adm" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="2adm, resolution 2.6&Aring;" />
-'''ADENINE-N6-DNA-METHYLTRANSFERASE TAQI'''<br />
-==Overview==
+==ADENINE-N6-DNA-METHYLTRANSFERASE TAQI==
-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.
+<StructureSection load='2adm' size='340' side='right'caption='[[2adm]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+== Structural highlights ==
+<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>
+</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>
+<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>
+<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>
+</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/ad/2adm_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=2adm ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-ADM 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 SAM as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entry 1ADM. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ADM OCA].
+*[[DNA methyltransferase 3D structures|DNA methyltransferase 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-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://ispc.weizmann.ac.il//pmbin/getpm?pmid=8995524 8995524]
+[[Category: Large Structures]]
-[[Category: Single protein]]
-[[Category: Site-specific DNA-methyltransferase (adenine-specific)]]
 [[Category: Thermus aquaticus]]
-[[Category: Saenger, W.]]
+[[Category: Saenger W]]
-[[Category: Schluckebier, G.]]
+[[Category: Schluckebier G]]
-[[Category: SAM]]
-[[Category: methyltransferase]]
-[[Category: restriction system]]
-[[Category: transferase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:03:58 2007''